|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-1199 |
0e+00 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 618.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSFKNTKlKIP--DGFTAILGPNGSGKSNTIDGICFVLGKTSAKSLRAGKFNQLItyHNGKRA---DYAEV 78
Cdd:TIGR02169 2 IERIELENFKSFGKKK-VIPfsKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLI--SNGKNGqsgNEAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 79 TLFFDNINREIPidsDKVGICRKVKLNGDNNYYVVWyevekqntkINTessqkktskaskvekrRRMKKNEVLDLLSKIS 158
Cdd:TIGR02169 79 TVTFKNDDGKFP---DELEVVRRLKVTDDGKYSYYY---------LNG----------------QRVRLSEIHDFLAAAG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 159 LIADGPNIILQGDLLRIIDTSPNERRKILDEVSGVAEFDEKSEKAKKELSQAREYIEKIDIRINEVRANLEKLKKEKEDA 238
Cdd:TIGR02169 131 IYPEGYNVVLQGDVTDFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 239 EKYTVYNKKLKVTKYILTSKKVEFLKMVLDETKDEIEALKETKNCYIQDISNIDSEIIGLKVKINELVNELNEKGSEEVM 318
Cdd:TIGR02169 211 ERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 319 ELHKSIKELEVNLNNDKNALENAIDDLKHTLKMEESKNNDLNETKEKINNIRIDTLKKEAEAKVLIKEIEKLNEERQNLE 398
Cdd:TIGR02169 291 RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 399 KKVEQSESQVKALKNQESKLSERINDTQKELYGLKNELNQLENTLNNRTFDYQKNNETIENLTNQIAEF-SDLEDT---- 473
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELeEEKEDKalei 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 474 KKLYKELEDIAVELEFSKKKLQEKITERNDSQSKLDNLHSEYVKENARIKTLKDMENFSldRAVKGVLDAKLPGVVDIAG 553
Cdd:TIGR02169 451 KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGG--RAVEEVLKASIQGVHGTVA 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 554 NLAKTKGEYKTAIEVAGGARLNHIVVKKMDDGSRAINYLKQKRLGRATFLPMDRIKGM--DAKDISDTGIIGKAIDLVEF 631
Cdd:TIGR02169 529 QLGSVGERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDErrDLSILSEDGVIGFAVDLVEF 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 632 DIKYTNVFKFIFGNTHIVDNLENAKKLSLKYkaRFVTLEGEVIEPSGAMVGGNIRRNSAIKVDIDMK-KLTNLSEDIKEL 710
Cdd:TIGR02169 609 DPKYEPAFKYVFGDTLVVEDIEAARRLMGKY--RMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPaELQRLRERLEGL 686
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 711 EQILSNVKDEIERLNNKINTCSTRKLELDNRLK-IARDQEFKKEEITKSNNlKIKELNMLNSKIDDEISELTDEKEILSQ 789
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGeIEKEIEQLEQEEEKLKE-RLEELEEDLSSLEQEIENVKSELKELEA 765
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 790 KVQNLDNKLSEVMGQRERIVNEIKSYENSELSKRIKEIDHKIRENESSKNTLENEIKKgAILVKEVLIPKISELNSNIKS 869
Cdd:TIGR02169 766 RIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRID 844
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 870 LADKKNMFKNSVEIYKSNIESNSSILSDKRGKYEELTKGLKDLTDKKECYELEIENLQNNKEELREKATDIDNQVNVINV 949
Cdd:TIGR02169 845 LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 950 DRAKYETRLEEEERKLYlcdtlENIEDISDEMIEETYSLEIDDLERnqallesSIKKLEPVNMRAIEDYDFINERYEELF 1029
Cdd:TIGR02169 925 KLEALEEELSEIEDPKG-----EDEEIPEEELSLEDVQAELQRVEE-------EIRALEPVNMLAIQEYEEVLKRLDELK 992
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1030 GKRKEYEQEEGKYLQLISEVQKRKKETFMKTYDRVAENYEQIYGEI-GGNGKLSLENEEDPFSGGLLIDASPMNKQLQNL 1108
Cdd:TIGR02169 993 EKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAELsGGTGELILENPDDPFAGGLELSAKPKGKPVQRL 1072
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1109 DVMSGGEKSLTALAFLFAIQRLNPSPFYVLDEVDAALDTKNASLIGDMISNASKESQFIVISHREQMISKSNVMYGVCM- 1187
Cdd:TIGR02169 1073 EAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIVVSLRSPMIEYADRAIGVTMr 1152
|
1210
....*....|..
gi 33578097 1188 ENGLSKIVSVKL 1199
Cdd:TIGR02169 1153 RNGESQVFGLKL 1164
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
4-1199 |
4.87e-168 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 523.73 E-value: 4.87e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSF-KNTKLKIPDGFTAILGPNGSGKSNTIDGICFVLGKTSAKSLRAGKFNQLItyHNG----KRADYAEV 78
Cdd:COG1196 3 LKRLELAGFKSFaDPTTIPFEPGITAIVGPNGSGKSNIVDAIRWVLGEQSAKSLRGGKMEDVI--FAGsssrKPLGRAEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 79 TLFFDNINREIPIDSDKVGICRKVKLNGDNNYYvvwyevekqntkINtessqkktskasKVEKRRRmkknEVLDLLSKIS 158
Cdd:COG1196 81 SLTFDNSDGTLPIDYDEVTITRRLYRSGESEYY------------IN------------GKPCRLK----DIQDLFLDTG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 159 LIADGPNIILQGDLLRIIDTSPNERRKILDEVSGVAEFDEKSEKAKKELSQAREYIEKIDIRINEVRANLEKLKKEKEDA 238
Cdd:COG1196 133 LGPESYSIIGQGMIDRIIEAKPEERRAIIEEAAGISKYKERKEEAERKLEATEENLERLEDILGELERQLEPLERQAEKA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 239 EKYTVYNKKLKVTKYILTSKKVEFLKMVLDETKDEIEALKETKNCYIQDISNIDSEIIGLKVKINELVNELNEKGSEEvM 318
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE-Y 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 319 ELHKSIKELEVNLNNDKNALENAIDDLKHTLKMEESKNNDLNETKEKINNIRIDTLKKEAEAKVLIKEIEKLNEERQNLE 398
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 399 KKVEQSESQVKALKNQESKLSERINDTQKELYGLKNELNQLENTLNNRTFDYQKNNETIENLTNQIAEfsDLEDTKKLYK 478
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE--EEEALEEAAE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 479 ELEDIAVELEFSKKKLQEKITERNDSQSKLDNLHSEYVKENARIKTLKDMENfSLDRAVKGVLDAKL----PGVVDIAGN 554
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA-DYEGFLEGVKAALLlaglRGLAGAVAV 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 555 LAKTKGEYKTAIEVAGGARLNHIVVKKMDDGSRAINYLKQKRLGRATFLPMDRIKGMDA-KDISDTGIIGKAIDLVEFDI 633
Cdd:COG1196 529 LIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAAlAAALARGAIGAAVDLVASDL 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 634 KYTNVFKFIFGNTHIVDNLENAKKLS-------LKYKARFVTLEGEVIEPSGAMVGGNIRRNSAikvdidmkkltNLSED 706
Cdd:COG1196 609 READARYYVLGDTLLGRTLVAARLEAalrravtLAGRLREVTLEGEGGSAGGSLTGGSRRELLA-----------ALLEA 677
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 707 IKELEQILSNVKDEIERLNNKintcstRKLELDNRLKIARDQEFKKEEitksnnlkikelnmlnskiddeiseltdekei 786
Cdd:COG1196 678 EAELEELAERLAEEELELEEA------LLAEEEEERELAEAEEERLEE-------------------------------- 719
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 787 lsqkvqnldnklsevmgqrerivneiksyenselskrikeidhkirenesskntleneikkgailvkevlipkiselnsn 866
Cdd:COG1196 --------------------------------------------------------------------------------
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 867 iksladkknmfknsveiyksniesnssilsdkrgkyeeltkglkdltdkkecyELEIENLQNNKEELREkatdidnqvnv 946
Cdd:COG1196 720 -----------------------------------------------------ELEEEALEEQLEAERE----------- 735
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 947 invdrakyetRLEEEERKLYLCDTLENIEDISDEMieetyslEIDDLERNQALLESSIKKLEPVNMRAIEDYDFINERYE 1026
Cdd:COG1196 736 ----------ELLEELLEEEELLEEEALEELPEPP-------DLEELERELERLEREIEALGPVNLLAIEEYEELEERYD 798
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1027 ELFGKRKEYEQEEGKYLQLISEVQKRKKETFMKTYDRVAENYEQIYGEI--GGNGKLSLENEEDPFSGGLLIDASPMNKQ 1104
Cdd:COG1196 799 FLSEQREDLEEARETLEEAIEEIDRETRERFLETFDAVNENFQELFPRLfgGGEAELLLTDPDDPLETGIEIMAQPPGKK 878
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1105 LQNLDVMSGGEKSLTALAFLFAIQRLNPSPFYVLDEVDAALDTKNASLIGDMISNASKESQFIVISHREQMISKSNVMYG 1184
Cdd:COG1196 879 LQRLSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDANVERFAELLKEMSEDTQFIVITHNKRTMEAADRLYG 958
|
1210
....*....|....*.
gi 33578097 1185 VCM-ENGLSKIVSVKL 1199
Cdd:COG1196 959 VTMqEPGVSRVVSVDL 974
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-1199 |
1.46e-158 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 504.59 E-value: 1.46e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSFKN-TKLKIPDGFTAILGPNGSGKSNTIDGICFVLGKTSAKSLRAGKFNQLItyHNG----KRADYAEV 78
Cdd:TIGR02168 2 LKKLELAGFKSFADpTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVI--FNGsetrKPLSLAEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 79 TLFFDNINREIP-IDSDKVGICRKVKLNGDNNYYvvwyevekqntkINtessqkktskasKVEKRRRmkknEVLDLLSKI 157
Cdd:TIGR02168 80 ELVFDNSDGLLPgADYSEISITRRLYRDGESEYF------------IN------------GQPCRLK----DIQDLFLDT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 158 SLIADGPNIILQGDLLRIIDTSPNERRKILDEVSGVAEFDEKSEKAKKELSQAREYIEKIDIRINEVRANLEKLKKEKED 237
Cdd:TIGR02168 132 GLGKRSYSIIEQGKISEIIEAKPEERRAIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 238 AEKYTVYNKKLKVTKYILTSKKVEFLKMVLDETKDEIEALKETKNCYIQDISNIDSEIIGLKVKINELVNELNEKGSE-- 315
Cdd:TIGR02168 212 AERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEly 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 316 ----EVMELHKSIKELEVNLNNDKNALENAIDDLKHTLKMEESKNNDLNETKEKInniriDTLKKEAEAkvLIKEIEKLN 391
Cdd:TIGR02168 292 alanEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL-----EELKEELES--LEAELEELE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 392 EERQNLEKKVEQSESQVKALKNQESKLSERINDTQKELYGLKNELNQLENTLNNRTFDYQKNNETIENltNQIAEFSDLE 471
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAEL 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 472 DTKKlyKELEDIAVELEFSKKKLQEKITERNDSQSKLDNLHSEYVKENARIKTLKDM-ENFS-LDRAVKGVLDAK--LPG 547
Cdd:TIGR02168 443 EELE--EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLqENLEgFSEGVKALLKNQsgLSG 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 548 VVDIAGNLAKTKGEYKTAIEVAGGARLNHIVVKKMDDGSRAINYLKQKRLGRATFLPMDRIKGMDAK------DISDTGI 621
Cdd:TIGR02168 521 ILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQgndreiLKNIEGF 600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 622 IGKAIDLVEFDIKYTNVFKFIFGNTHIVDNLENAKKL--SLKYKARFVTLEGEVIEPSGAMVGG-NIRRNSAIKVDIDMK 698
Cdd:TIGR02168 601 LGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELakKLRPGYRIVTLDGDLVRPGGVITGGsAKTNSSILERRREIE 680
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 699 KLTN----LSEDIKELEQILSNVKDEIERLNNKINTCSTRKLELDNRLKIARDQEFKKEEITKSNNLKIKELNMLNSKID 774
Cdd:TIGR02168 681 ELEEkieeLEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 775 DEISELTDEKEILSQKVQNLDNKLSEVMGQRERIVNEIKS--YENSELSKRIKEIDHKIRENESSKNTLENEIKKGAILV 852
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlrEALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 853 kEVLIPKISELNSNIKSLADKKNMFKNSVEIYKSNIESNSSILSDKRGKYEELTKGLKDLTDKKECYELEIENLQNNKEE 932
Cdd:TIGR02168 841 -EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 933 LREKATDIDNQVNVINVDRAKYETRLEEEERklylcDTLENIEDIsdemiEETYSLEIDDLERNQALLESSIKKLEPVNM 1012
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDNLQERLSEEYS-----LTLEEAEAL-----ENKIEDDEEEARRRLKRLENKIKELGPVNL 989
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1013 RAIEDYDFINERYEELFGKRKEYEQEEGKYLQLISEVQKRKKETFMKTYDRVAENYEQIYGEI--GGNGKLSLENEEDPF 1090
Cdd:TIGR02168 990 AAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRVFPKLfgGGEAELRLTDPEDLL 1069
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1091 SGGLLIDASPMNKQLQNLDVMSGGEKSLTALAFLFAIQRLNPSPFYVLDEVDAALDTKNASLIGDMISNASKESQFIVIS 1170
Cdd:TIGR02168 1070 EAGIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLLKEFSKNTQFIVIT 1149
|
1210 1220 1230
....*....|....*....|....*....|
gi 33578097 1171 HREQMISKSNVMYGVCMEN-GLSKIVSVKL 1199
Cdd:TIGR02168 1150 HNKGTMEVADQLYGVTMQEkGVSKIVSVDL 1179
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
4-1190 |
8.65e-107 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 363.52 E-value: 8.65e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSFKNTK-LKIPDGFTAILGPNGSGKSNTIDGICFVLGKTSAKSLRAGKFNQLITYHNGKRADYAEVTLFF 82
Cdd:pfam02463 2 LKRIEIEGFKSYAKTViLPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIHSKSGAFVNSAEVEITF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 83 DNINREIPIDSDKVGICRKVKLNGDNNYYVvwyevekqntkintessqkktskaskveKRRRMKKNEVLDLLSKISLIAD 162
Cdd:pfam02463 82 DNEDHELPIDKEEVSIRRRVYRGGDSEYYI----------------------------NGKNVTKKEVAELLESQGISPE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 163 GPNIILQGDLLRIIDTSPNERRKILDEVSGVAEFDEKSEKAKKELSQAREYIEKIDIRINEVRANLEKLKKEKEDAEKYT 242
Cdd:pfam02463 134 AYNFLVQGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 243 VYNKKLKVTK-YILTSKKVEFLKMVLDETKDEIEALKETKNCYIQDISNIDSEIIGLKvkiNELVNELNEKGSEEVMELH 321
Cdd:pfam02463 214 QLKEKLELEEeYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVL---KENKEEEKEKKLQEEELKL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 322 KSIKELEVNLNNDKNALENAIDDLKHTLKMEESKNNDLNETKEKINNIRIDTLKKEAEAKVLIKEIEKLNEERQNLEKKV 401
Cdd:pfam02463 291 LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQ 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 402 EQSESQVKALKNQESKLSERINDTQKELYGLKNELNQLENTLNNRTFDYQKNNETIENLTNQIAEFSDLEdTKKLYKELE 481
Cdd:pfam02463 371 LEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIE-LKQGKLTEE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 482 DIAVELEFSKKKLQEKITERNDSQSKLDNLHSEYVKENARIKTLKDMENFSLDRAVKGVLDAKLPGVVDIAGNLAKTKGE 561
Cdd:pfam02463 450 KEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHG 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 562 YKTAIEVAGGARLNHIVVKKMDDGSRAINYLKQKRLGRATFLPMDRIKGMDAKDISDTGIIGKAIDLVEFDI---KYTNV 638
Cdd:pfam02463 530 RLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPilnLAQLD 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 639 FKFIFGNTHIVDNLENAKKLSLKYKARFVTLEGEVIEPSGAMVGGNIRRNSAIKVDIDMKKLT---NLSEDIKELEQILS 715
Cdd:pfam02463 610 KATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTkelLEIQELQEKAESEL 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 716 NVKDEIERLNNKINTCSTRKLEL-DNRLKIARDQEFKKEEITKSNNLKIKELNMLNSKIDDEISELTDEKEILSQKVQNL 794
Cdd:pfam02463 690 AKEEILRRQLEIKKKEQREKEELkKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSEL 769
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 795 DNKLSEVMGQRERIVNEIKSYENSELSKRIKEIDHKIRENESSKNTLENEIKKGAILVKEVLIPKISELNSNIKSLADKK 874
Cdd:pfam02463 770 SLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLE 849
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 875 NMFKNSVEIYKSNIESNSSILSDKRGKYEELTKGLKDLTDKKECYELEIENLQNNKEELREKATDIDNQVNVINVDRAKY 954
Cdd:pfam02463 850 KLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEI 929
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 955 ETRLEEEERKLYLCDTLENIEDISDemieetysleIDDLERNQALLESSIKKLEPVNMRAIEDYDFINERYEELFGKRKE 1034
Cdd:pfam02463 930 LLKYEEEPEELLLEEADEKEKEENN----------KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKER 999
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1035 YEQEEGKYLQLISEVQKRKKETFMKTYDRVA--ENYEQIYGEIGGNGKLSLENEEDPFSGGLLIDASPMNKQLQNLDVMS 1112
Cdd:pfam02463 1000 LEEEKKKLIRAIIEETCQRLKEFLELFVSINkgWNKVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLS 1079
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33578097 1113 GGEKSLTALAFLFAIQRLNPSPFYVLDEVDAALDTKNASLIGDMISNASKESQFIVISHREQMISKSNVMYGVCMENG 1190
Cdd:pfam02463 1080 GGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVEN 1157
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1102-1193 |
1.58e-44 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 159.94 E-value: 1.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1102 NKQLQNLDVMSGGEKSLTALAFLFAIQRLNPSPFYVLDEVDAALDTKNASLIGDMISNASKESQFIVISHREQMISKSNV 1181
Cdd:cd03278 105 GKKVQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADR 184
|
90
....*....|...
gi 33578097 1182 MYGVCMEN-GLSK 1193
Cdd:cd03278 185 LYGVTMQEsGVSK 197
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
4-88 |
5.45e-34 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 129.51 E-value: 5.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSF-KNTKLKIPDGFTAILGPNGSGKSNTIDGICFVLGKTSAKSLRAGKFNQLITYHNGKR--ADYAEVTL 80
Cdd:cd03278 1 LKKLELKGFKSFaDKTTIPFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKSLRGEKMSDVIFAGSETRkpANFAEVTL 80
|
....*...
gi 33578097 81 FFDNINRE 88
Cdd:cd03278 81 TFDNSDGR 88
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
546-658 |
1.75e-33 |
|
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 214944 [Multi-domain] Cd Length: 120 Bit Score: 125.42 E-value: 1.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 546 PGVVDIAGNLAKTKGEYKTAIEVAGGARLNHIVVKKMDDGSRAINYLKQKRLGRATFLPMDRIKG-------MDAKDISD 618
Cdd:smart00968 1 PGVLGRVADLISVDPKYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPrspagskLREALLPE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 33578097 619 TGIIGKAIDLVEFDIKYTNVFKFIFGNTHIVDNLENAKKL 658
Cdd:smart00968 81 PGFVGPAIDLVEYDPELRPALEYLLGNTLVVDDLETARRL 120
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
545-659 |
1.72e-30 |
|
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 461926 [Multi-domain] Cd Length: 116 Bit Score: 116.59 E-value: 1.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 545 LPGVVDIAGNLAKTKGEYKTAIEVAGGARLNHIVVKKMDDGSRAINYLKQKRLGRATFLPMDRIKGMDAKDISDTGI-IG 623
Cdd:pfam06470 1 LKGVLGRLADLIEVDEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKPRPRRPGADLKGgAG 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 33578097 624 KAIDLVEFDIKYTNVFKFIFGNTHIVDNLENAKKLS 659
Cdd:pfam06470 81 PLLDLVEYDDEYRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1110-1193 |
2.37e-27 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 109.71 E-value: 2.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1110 VMSGGEKSLTALAFLFAIQRLNPSPFYVLDEVDAALDTKNASLIGDMI-SNASKESQFIVISHREQMISKSNVMYGVCME 1188
Cdd:cd03239 94 ILSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIkEMAKHTSQFIVITLKKEMFENADKLIGVLFV 173
|
....*
gi 33578097 1189 NGLSK 1193
Cdd:cd03239 174 HGVST 178
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1099-1199 |
4.77e-26 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 108.43 E-value: 4.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1099 SPMNKQLQNLDVMSGGEKSLTALAFLFAIQRLNPSPFYVLDEVDAALDTKNASLIGDMI-SNASKESQFIVISHREQMIS 1177
Cdd:cd03275 144 NPPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIrEQAGPNFQFIVISLKEEFFS 223
|
90 100
....*....|....*....|....
gi 33578097 1178 KSNVMYGVCMENG--LSKIVSVKL 1199
Cdd:cd03275 224 KADALVGVYRDQEcnSSKVLTLDL 247
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1106-1194 |
1.09e-22 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 98.49 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1106 QNLDVMSGGEKSLTALAFLFAIQRLNPSPFYVLDEVDAALDTKNASLIGDMISNASKESQFIVISHREQMISKSNVMYGV 1185
Cdd:cd03272 154 QEMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVADKFYGV 233
|
....*....
gi 33578097 1186 CMENGLSKI 1194
Cdd:cd03272 234 KFRNKVSTI 242
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1103-1195 |
1.68e-21 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 94.28 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1103 KQLQNLdvmSGGEKSLTALAFLFAIQRLNPSPFYVLDEVDAALDTKNASLIGDMISNASKESQFIVISHREQMISKSNVM 1182
Cdd:cd03274 123 KNISNL---SGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELADRL 199
|
90
....*....|...
gi 33578097 1183 YGVCMENGLSKIV 1195
Cdd:cd03274 200 VGIYKTNNCTKSV 212
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1106-1194 |
7.84e-21 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 93.13 E-value: 7.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1106 QNLDVMSGGEKSLTALAFLFAIQRLNPSPFYVLDEVDAALDTKNASLIGDMISNASKESQFIVISHREQMISKSNVMYGV 1185
Cdd:cd03273 162 ESLTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNANVLFRT 241
|
....*....
gi 33578097 1186 CMENGLSKI 1194
Cdd:cd03273 242 RFVDGTSTV 250
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1111-1193 |
1.34e-20 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 89.73 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1111 MSGGEKSLTALAFLFAIQRLNPSPFYVLDEVDAALDTKNASLIGDMI-SNASKESQFIVISHREQMISKSNVMYGV-CME 1188
Cdd:cd03227 78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAIlEHLVKGAQVIVITHLPELAELADKLIHIkKVI 157
|
....*
gi 33578097 1189 NGLSK 1193
Cdd:cd03227 158 TGVYK 162
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
4-527 |
8.87e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 89.33 E-value: 8.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSFKNTKLKIPDGFTAILGPNGSGKSNTIDGICFVLGKTSAKSlraGKFNQLITyhngKRADYAEVTLFFD 83
Cdd:PRK02224 3 FDRVRLENFKCYADADLRLEDGVTVIHGVNGSGKSSLLEACFFALYGSKALD---DTLDDVIT----IGAEEAEIELWFE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 84 NINREIPIDsdkvgicRKVKLNGDNnyyvvwyeveKQNTKINTESSQKKTSKASKVEKrrrmkknEVLDLLSKISLIADG 163
Cdd:PRK02224 76 HAGGEYHIE-------RRVRLSGDR----------ATTAKCVLETPEGTIDGARDVRE-------EVTELLRMDAEAFVN 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 164 PNIILQGDLLRIIDTSPNERRKILDEVSGVAEFDEKSEKAkkelSQAREYIEKIdirINEVRANLEKLKK---EKEDAEK 240
Cdd:PRK02224 132 CAYVRQGEVNKLINATPSDRQDMIDDLLQLGKLEEYRERA----SDARLGVERV---LSDQRGSLDQLKAqieEKEEKDL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 241 YTVYN---KKLKVTKYILT--SKKVEFLKMVLDETKDEIEALKETKncyiQDISNIDSEIIGLKVKINELVNElNEKGSE 315
Cdd:PRK02224 205 HERLNgleSELAELDEEIEryEEQREQARETRDEADEVLEEHEERR----EELETLEAEIEDLRETIAETERE-REELAE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 316 EVMELHKSIKELEVNLNN----------DKNALENAIDDL---KHTLKME-ESKNNDLNETKEKINNIRIDTLKKEAEAK 381
Cdd:PRK02224 280 EVRDLRERLEELEEERDDllaeaglddaDAEAVEARREELedrDEELRDRlEECRVAAQAHNEEAESLREDADDLEERAE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 382 VLIKEIEKLNEERQNLEKKVEQSESQVKALKNQESKLSERINDTQKELYGLKNELNQLENTLNNRTFDYQKNNETIENLT 461
Cdd:PRK02224 360 ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTAR 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33578097 462 NQIAEFSDLEDTKK---LYKELED--IAVELEFSKKKLQEKITERNDSQSKLDNLHS------EYVKENARIKTLKD 527
Cdd:PRK02224 440 ERVEEAEALLEAGKcpeCGQPVEGspHVETIEEDRERVEELEAELEDLEEEVEEVEErleraeDLVEAEDRIERLEE 516
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
4-192 |
2.49e-16 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 80.03 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSFKnTKLKIPD---GFTAILGPNGSGKSNTIDGICFVLGKTSAKSLRAGKFNQLItYHNGKRA-DYAEVT 79
Cdd:cd03273 3 IKEIILDGFKSYA-TRTVISGfdpQFNAITGLNGSGKSNILDAICFVLGITNLSTVRASNLQDLI-YKRGQAGiTKASVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 80 LFFDNINR-EIPI---DSDKVGICRKVKLNGDNNYYvvwyevekqntkINTESSQKKTskaskvekrrrmkkneVLDLLS 155
Cdd:cd03273 81 IVFDNSDKsQSPIgfeNYPEITVTRQIVLGGTNKYL------------INGHRAQQQR----------------VQDLFQ 132
|
170 180 190
....*....|....*....|....*....|....*...
gi 33578097 156 KISLIADGPN-IILQGDLLRIIDTSPNERRKiLDEVSG 192
Cdd:cd03273 133 SVQLNVNNPHfLIMQGRITKVLNMGGVWKES-LTELSG 169
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
4-86 |
9.37e-14 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 70.80 E-value: 9.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSFKN-TKLKIPDGFTAILGPNGSGKSNTIDGICFVLGKTSAKSLRAGKfnqLITYHNGKRAD--YAEVTL 80
Cdd:cd03239 1 IKQITLKNFKSYRDeTVVGGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSL---LFLAGGGVKAGinSASVEI 77
|
....*.
gi 33578097 81 FFDNIN 86
Cdd:cd03239 78 TFDKSY 83
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
4-86 |
1.72e-13 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 70.79 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSFKNTKLKIP--DGFTAILGPNGSGKSNTIDGICFVLGKtSAKSLRAGKFNQLItyHNGKR---ADYAEV 78
Cdd:cd03274 3 ITKLVLENFKSYAGEQVIGPfhKSFSAIVGPNGSGKSNVIDSMLFVFGF-RASKMRQKKLSDLI--HNSAGhpnLDSCSV 79
|
....*...
gi 33578097 79 TLFFDNIN 86
Cdd:cd03274 80 EVHFQEII 87
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
4-82 |
3.53e-13 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 70.68 E-value: 3.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSFKNTKLKIP-DGFTAILGPNGSGKSNTIDGICFVLGKTSAkSLRAGKFNQLI-TYHNGKR-ADYAEVTL 80
Cdd:cd03275 1 LKRLELENFKSYKGRHVIGPfDRFTCIIGPNGSGKSNLMDAISFVLGEKSS-HLRSKNLKDLIyRARVGKPdSNSAYVTA 79
|
..
gi 33578097 81 FF 82
Cdd:cd03275 80 VY 81
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
4-106 |
1.56e-12 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 70.57 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSFKNTKLKIPDGFTAILGPNGSGKSNTIDGICFVlgkTSAKSLRAGKFNQLITYHngkrADYAEVTLFFD 83
Cdd:COG1195 2 LKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAIYLL---ATGRSFRTARDAELIRFG----ADGFRVRAEVE 74
|
90 100
....*....|....*....|....*.
gi 33578097 84 NINREIPID---SDKVGicRKVKLNG 106
Cdd:COG1195 75 RDGREVRLGlglSRGGK--KRVRING 98
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
4-530 |
1.85e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.55 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSFKNTKLKIPDGFTAILGPNGSGKSNTIDGICFVLGKTSAKSLRAGKFNQLItyHNGKRAdyAEVTLFFD 83
Cdd:PRK03918 3 IEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFT--RIGGSG--TEIELKFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 84 NinreipiDSDKVGICRKVKLNGDNNYYVVWYEVEKQNTKINTESSQK--------------KTSKASKVEKRRRMKKne 149
Cdd:PRK03918 79 K-------NGRKYRIVRSFNRGESYLKYLDGSEVLEEGDSSVREWVERlipyhvflnaiyirQGEIDAILESDESREK-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 150 vldLLSKISLIADGPNIilQGDLLRIIDTSPNERRKILDEVSGVAEFDEKSEKAKKELSQAREYIEKIDIRINEVRANLE 229
Cdd:PRK03918 150 ---VVRQILGLDDYENA--YKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 230 KLKKEKEDAEKytvynkklkvTKYILTSKKVEFLKMvldetKDEIEALKEtkncyiqDISNIDSEIIGLKVKINEL---- 305
Cdd:PRK03918 225 KLEKEVKELEE----------LKEEIEELEKELESL-----EGSKRKLEE-------KIRELEERIEELKKEIEELeekv 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 306 --VNELNEKGSE--EVMELHKSIKELEVNLNNDKNALENAIDDLKHTLKMEESKNNDLNETKEKINNI--RIDTLKKEAE 379
Cdd:PRK03918 283 keLKELKEKAEEyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELekRLEELEERHE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 380 ----------------AKVLIKEIEKLNEERQNLEKKVEQSESQVKALKNQESKLSERINDTQKELYGLKN--------- 434
Cdd:PRK03918 363 lyeeakakkeelerlkKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcg 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 435 -----------------ELNQLENTLNNRTFDYQKNNETIENLTNQIAEFSDLEDTKKLYKELEDIAVELE-FSKKKLQE 496
Cdd:PRK03918 443 relteehrkelleeytaELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKkYNLEELEK 522
|
570 580 590
....*....|....*....|....*....|....
gi 33578097 497 KITERNDSQSKLDNLHSEYVKENARIKTLKDMEN 530
Cdd:PRK03918 523 KAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKK 556
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
261-847 |
2.72e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.40 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 261 EFLK-MVLDE--TKDEIEALKEtkncYIQDISNIDSEIIGLKVKINELvnelnekgsEEVMELHKSIKELEVNLNndkna 337
Cdd:COG4913 211 DFVReYMLEEpdTFEAADALVE----HFDDLERAHEALEDAREQIELL---------EPIRELAERYAAARERLA----- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 338 lenAIDDLKHTLkmeesknndlnetkekinniriDTLKKEAEAKVLIKEIEKLNEERQNLEKKVEQSESQVKALKNQESK 417
Cdd:COG4913 273 ---ELEYLRAAL----------------------RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 418 LSERINDTQ-KELYGLKNELNQLENTLNNRTFDYQKNNETIENLtnQIAEFSDLEDTKKLYKELEDIAVELEFSKKKLQE 496
Cdd:COG4913 328 LEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAAL--GLPLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 497 KITERNDSQSKLDNLHSEYVKENARIKTLKDmenfSLDRAVK----------GVLDAKLPgvvdIAGNLAKTKGEYK--- 563
Cdd:COG4913 406 ALAEAEAALRDLRRELRELEAEIASLERRKS----NIPARLLalrdalaealGLDEAELP----FVGELIEVRPEEErwr 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 564 TAIEVA-GGARLNHIV-VKKMDDGSRAINYLKQKrlGRATFlpmDRIKGMDAKD----ISDTGIIGKaidlVEFDI-KYT 636
Cdd:COG4913 478 GAIERVlGGFALTLLVpPEHYAAALRWVNRLHLR--GRLVY---ERVRTGLPDPerprLDPDSLAGK----LDFKPhPFR 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 637 NVFKFIFGNT---HIVDNLENakklsLKYKARFVTLEGeviepsgaMVGGN-----------IRRNSAIKVDIDmKKLTN 702
Cdd:COG4913 549 AWLEAELGRRfdyVCVDSPEE-----LRRHPRAITRAG--------QVKGNgtrhekddrrrIRSRYVLGFDNR-AKLAA 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 703 LSEDIKELEQILSNVKDEIERLNNKINTCSTRKLELDN--------------RLKIARDQEfKKEEITKSNN----LKiK 764
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeidvasaEREIAELEA-ELERLDASSDdlaaLE-E 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 765 ELNMLNSKIDD---EISELTDEKEILSQKVQNLDNKLSEVMGQRERIVNEIKSYENSELSKRIKEIDHKIRENESSKNtL 841
Cdd:COG4913 693 QLEELEAELEEleeELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREN-L 771
|
....*.
gi 33578097 842 ENEIKK 847
Cdd:COG4913 772 EERIDA 777
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
4-86 |
4.86e-11 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 66.11 E-value: 4.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSFKNTKLKIPDgFTAILGPNGSGKSNTIDGICFvLGKTSAKSLRA-----GKFNQLITYHNGKRADYAEV 78
Cdd:COG4637 2 ITRIRIKNFKSLRDLELPLGP-LTVLIGANGSGKSNLLDALRF-LSDAARGGLQDalarrGGLEELLWRGPRTITEPIRL 79
|
....*...
gi 33578097 79 TLFFDNIN 86
Cdd:COG4637 80 ELEFAEED 87
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
195-534 |
1.36e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.81 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 195 EFDEKSEKAKKELSQAREYIEKIDIRINEVRANLEKLKKEKEDAEKytvyNKKLKVTKYILTSKKVEFLKMVLDETKDEI 274
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES----ENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 275 EALKETKNCYIQDISNID--SEIIGLKVKINELVNELNEKGSEEVMELHKSIKELEVNLNNDKNALENAIDDLKHTlkmE 352
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEklNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNT---R 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 353 ESKNNDLNETKEKINNIRIDTLKKEAEAKVLIKEIEKLNEERQNLEKKVEQSESQVKALKNQESKLSERINDTQKELYGL 432
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 433 KNELNQLENTLNNRTFDYQK--NNETIENLTNqiaefsDLEDTKKLYKELEDIAVELEFSKKKLQEKITERNDSQSKLDN 510
Cdd:TIGR04523 544 EDELNKDDFELKKENLEKEIdeKNKEIEELKQ------TQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEK 617
|
330 340
....*....|....*....|....
gi 33578097 511 LHSEYVKENARIKTLKDMENFSLD 534
Cdd:TIGR04523 618 ELEKAKKENEKLSSIIKNIKSKKN 641
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
354-527 |
1.36e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.79 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 354 SKNNDLNETKEKINNIRIDTLKKEAEAKVLIKEIEKLNEERQNLEKKVEQSESQVKALKNQESKLSERINDTQKELYGLK 433
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 434 NELNQLENTLNNRTFDYQKN--NETIENLTNQiAEFSDLEDTKKLYKEL----EDIAVELEFSKKKLQEKITERNDSQSK 507
Cdd:COG4942 97 AELEAQKEELAELLRALYRLgrQPPLALLLSP-EDFLDAVRRLQYLKYLaparREQAEELRADLAELAALRAELEAERAE 175
|
170 180
....*....|....*....|
gi 33578097 508 LDNLHSEYVKENARIKTLKD 527
Cdd:COG4942 176 LEALLAELEEERAALEALKA 195
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
4-231 |
1.47e-10 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 61.95 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSFKNT-KLKIPDGFTAILGPNGSGKSNTIDGICFVL-GKTSAkslRAGKFNQLITyhngKRADYAEVTLF 81
Cdd:COG0419 2 LLRLRLENFRSYRDTeTIDFDDGLNLIVGPNGAGKSTILEAIRYALyGKARS---RSKLRSDLIN----VGSEEASVELE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 82 FDNINREipidsdkvgicrkvklngdnnyyvvwYEVEKQntkintessqkktskaskvekrrrmkknevldllskislia 161
Cdd:COG0419 75 FEHGGKR--------------------------YRIERR----------------------------------------- 87
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 162 dgpniilQGDLLRIIDTSPNERRKILDEVSGVAEFDEKSEKAKKELSQAREYIEKIDIRINEVRANLEKL 231
Cdd:COG0419 88 -------QGEFAEFLEAKPSERKEALKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQL 150
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1-420 |
5.54e-10 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 63.49 E-value: 5.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1 MISISEIHLKNFKSFKNTKLKIP-DGF--TAILGPNGSGKSNTIDGICFVLgktSAKSLRAGKFNQLITYHNGKRAdYAE 77
Cdd:PHA02562 1 MLKFKKIRYKNILSVGNQPIEIQlDKVkkTLITGKNGAGKSTMLEALTFAL---FGKPFRDIKKGQLINSINKKDL-LVE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 78 VtlffdninrEIPIDSDKVGICRKVKLNgdnnyyvvWYEVEKQNTKINTESSQKKTSKAskvekrrrmkknevLDLLSKI 157
Cdd:PHA02562 77 L---------WFEYGEKEYYIKRGIKPN--------VFEIYCNGKLLDESASSKDFQKY--------------FEQMLGM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 158 SLIADGPNIIL-QGDLLRIIDTSPNERRKILDEVSGVAEFDEKSEKAKKELSQAREYIEKIDIRINEVRANLEKLKKEKE 236
Cdd:PHA02562 126 NYKSFKQIVVLgTAGYVPFMQLSAPARRKLVEDLLDISVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 237 DAEKYTVYNKKLKVTKYILTSKKVEFLKMVLDETKDEIEALKETKNCYIQDISNIDSEIIGLKVKINELVNELN------ 310
Cdd:PHA02562 206 EQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekgg 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 311 ---------EKGSEEVMELHKSIKELEVNLNndknALENAIDDLKHTLKMEESKNNDLNETKEKINNIRIDTLKKEAEAK 381
Cdd:PHA02562 286 vcptctqqiSEGPDRITKIKDKLKELQHSLE----KLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAK 361
|
410 420 430
....*....|....*....|....*....|....*....
gi 33578097 382 VLIKEIEKLNEERQNLEKKVEQSESQVKALKNQESKLSE 420
Cdd:PHA02562 362 KVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVK 400
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
214-886 |
6.25e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.50 E-value: 6.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 214 IEKIDIRINEVRANLEKLKKE---KEDAEKYTVYNKKLKVTKYILTSKKVEFLKMVLDETKDEIEALKETKNCYIQDISN 290
Cdd:TIGR04523 28 ANKQDTEEKQLEKKLKTIKNElknKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 291 IDSEIIGLKVKINELVNELN--EKGSEEVMELHKSIKELEVNLNNDKNALENAIDDLKHTLKMEESKNNDLNETKEKINN 368
Cdd:TIGR04523 108 INSEIKNDKEQKNKLEVELNklEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 369 IRIDTLKKEAEAKVLIKEIEKLNEERQNLEKKVEQSESQVKALKNQESKLSERIND-------TQKELYGLKNELNQLEN 441
Cdd:TIGR04523 188 NIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEktteisnTQTQLNQLKDEQNKIKK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 442 TLNNRTFDYQKNNETIENLTNQI----AEFSDLEDTKK--LYKELEDIAVELEFSKKKLQEKITERNDSQSKLDNLHSEY 515
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLnqlkSEISDLNNQKEqdWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 516 VKEnariKTLKDMENFSLDRAVKGVLDAklpgvvdiAGNLAKTKGEYKTAIEvaggarlnhivvkkmddgsraiNYLKQK 595
Cdd:TIGR04523 348 KKE----LTNSESENSEKQRELEEKQNE--------IEKLKKENQSYKQEIK----------------------NLESQI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 596 RLGRATFLPMDRIkgmdaKDISDTGIIGKAIDLVEFDIKYTNVFKFIFGNTHIVDNLEN---AKKLSLKYKARFVTLEGE 672
Cdd:TIGR04523 394 NDLESKIQNQEKL-----NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNqdsVKELIIKNLDNTRESLET 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 673 VIEPSGAMVgGNIRRNSAIKV---DIDMKKLTNLSEDIKELEQILSNVKDEIERLNNKINTCSTRKLELDNRLKiardqE 749
Cdd:TIGR04523 469 QLKVLSRSI-NKIKQNLEQKQkelKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKIS-----D 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 750 FKKEEITKSNNLKIKELNMLNSKIDDEISELTDEKEILSQKVQNLDNKLSEVMGQRERIVNEIKSYEN--SELSKRIKEI 827
Cdd:TIGR04523 543 LEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKkiSSLEKELEKA 622
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33578097 828 DHKIRENESSKNTLE---NEIKKGAILVKEVL---IPKISELNSNIKSLADKKNMFKNSVEIYKS 886
Cdd:TIGR04523 623 KKENEKLSSIIKNIKskkNKLKQEVKQIKETIkeiRNKWPEIIKKIKESKTKIDDIIELMKDWLK 687
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
1102-1170 |
1.39e-09 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 59.53 E-value: 1.39e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33578097 1102 NKQLQNLD--VMSGGEKSLTALAFLFAIQRLNPSPFYVLDEVDAALDTKNASLIGDMISNASKE---SQFIVIS 1170
Cdd:cd03277 116 GEQLQELDphHQSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETACKegtSQYFLIT 189
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
353-529 |
1.90e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.00 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 353 ESKNNDLNETKEKINNIRIDTLKKEAEAKVLIKEIEKLNEERQNLEKKVEQSESQVKALKNQESKLSERINDTQKELYGL 432
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 433 KNELNQLENTLNNRTFDyqknnETIENLT--NQIAEFSD--LEDTKKLYKELEDIAVELEFSKKKLQEKITERNDSQSKL 508
Cdd:COG3883 99 GGSVSYLDVLLGSESFS-----DFLDRLSalSKIADADAdlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180
....*....|....*....|.
gi 33578097 509 DNLHSEYVKENARIKTLKDME 529
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAA 194
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
182-518 |
2.84e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 182 ERRKILDEVSGVAEFDEKSEKAKKELSQAREYIEKIDIRINEVRANLEKLKKEKEDAEKYTVYNKKLKVTKYILTSKKVE 261
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 262 FLKMVLDETKDEIEALKETKNCYIQDISNIDSEIIGLKVKINELVN-----------------ELNEKGSEEVMELH--- 321
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaieelkkakgkcpvcgrELTEEHRKELLEEYtae 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 322 --------KSIKELEVNLNNDKNALENAIDDLKHTLKMEESKnNDLNETKEKINNIRIDTLKKEAEakvlikEIEKLNEE 393
Cdd:PRK03918 461 lkriekelKEIEEKERKLRKELRELEKVLKKESELIKLKELA-EQLKELEEKLKKYNLEELEKKAE------EYEKLKEK 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 394 RQNLEKKVEQSESQVKALKNQESKLSErindTQKELYGLKNELNQLENTLNNRTF-DYQKNNETIENLTNQIAEFSDLED 472
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLEELKKKLAE----LEKKLDELEEELAELLKELEELGFeSVEELEERLKELEPFYNEYLELKD 609
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 33578097 473 TKK----LYKELEDIAVELEFSKKKLQEKITERNDSQSKLDNLHSEYVKE 518
Cdd:PRK03918 610 AEKelerEEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE 659
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
691-1037 |
3.45e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.21 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 691 IKVDIDMKKLTNLSEDIKELEQILSNVKDEIERLNNKINTCSTRKLELDNRLKiarDQEFKKEEITksnnlkikELNMLN 770
Cdd:PRK02224 192 LKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLE---EHEERREELE--------TLEAEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 771 SKIDDEISELTDEKEILSQKVQNLDNKLSEVMGQRERIVN---------EIKSYENSELSKRIKEIDHKIRENESSKNTL 841
Cdd:PRK02224 261 EDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAeaglddadaEAVEARREELEDRDEELRDRLEECRVAAQAH 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 842 ENEIKKgailvkevlipkiseLNSNIKSLADKKNMFKNSVEIYKSNIESNSSILSDKRGKYEELTKGLKDLTDKKECYEL 921
Cdd:PRK02224 341 NEEAES---------------LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 922 EIENLQNNKEELREKATDIDNQVNVINVDRAKYETRLEEEERKLYLCDTLENIEDISDEMIEET---YSLEIDDLERNQA 998
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETieeDRERVEELEAELE 485
|
330 340 350
....*....|....*....|....*....|....*....
gi 33578097 999 LLESSIKKLEPVNMRAiEDYDFINERYEELFGKRKEYEQ 1037
Cdd:PRK02224 486 DLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEE 523
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
331-526 |
3.59e-09 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 59.33 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 331 LNNDKNALENAiDDLKHTLKMEESKN-NDLNETKEKINNIRIDTLKKEAEAKVLIKEIEKLNEERQNLEKKVEQSESQVK 409
Cdd:pfam15294 79 LQADISELENR-ELLEQIAEFEEREFtSSNKKPNFELNKPKLEPLNEGGGSALLHMEIERLKEENEKLKERLKTLESQAT 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 410 ALKNQESKLSERINDTQKELYGLKN------ELNQLENTLNNRTFDYQKNNETIENLTNQIAEfsDLEDTKKLYKELEDi 483
Cdd:pfam15294 158 QALDEKSKLEKALKDLQKEQGAKKDvksnlkEISDLEEKMAALKSDLEKTLNASTALQKSLEE--DLASTKHELLKVQE- 234
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 33578097 484 avELEFSKKKLQEKITErndsQSKLDNLHSEYVKENARIKTLK 526
Cdd:pfam15294 235 --QLEMAEKELEKKFQQ----TAAYRNMKEMLTKKNEQIKELR 271
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
687-1198 |
4.25e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 61.07 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 687 RNSAIKVDIDMKKLTNLSEDIKELEQILSNVKDEIERLNNKINTCSTRKLELDNRLKIARDQEFKKEEITKsnnlkiKEL 766
Cdd:PRK01156 338 YNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIK------KEL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 767 NMLNSKIDD---EISELTDEKEILSQKVQNLDNKLSEVMGQR----------ERIVNEIKSYENSELSKRIKEIDH---- 829
Cdd:PRK01156 412 NEINVKLQDissKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgttlgEEKSNHIINHYNEKKSRLEEKIREieie 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 830 --KIRENESSKNTLENEIKKGAILVKEVLIPKISELNSNIKSLADKKNMFKNSVEIYKSNIESNSSI-LSDKRGKYEELT 906
Cdd:PRK01156 492 vkDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLkLEDLDSKRTSWL 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 907 KGLKDLTDkkecyeLEIENLQNNKEELREKATDIDNQVNVINVDRAKYETRLEEEERKLYlcDTLENIEDISDEMIE--- 983
Cdd:PRK01156 572 NALAVISL------IDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIE--NEANNLNNKYNEIQEnki 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 984 --ETYSLEIDDLERNQALLESSIKKLEPVNMRAIE---DYDFINERYEELFGKRKEYEQEEGKYLQLISEVQKR-----K 1053
Cdd:PRK01156 644 liEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDiedNLKKSRKALDDAKANRARLESTIEILRTRINELSDRindinE 723
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1054 KETFMKTYDRVAENYEQIYGEIGGNGKLSLENEEDP-----------FSGGLLIDASPMNKQL----------QNLDVMS 1112
Cdd:PRK01156 724 TLESMKKIKKAIGDLKRLREAFDKSGVPAMIRKSASqamtsltrkylFEFNLDFDDIDVDQDFnitvsrggmvEGIDSLS 803
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1113 GGEKSLTALAFLFAIQR--LNPSPFYVLDEVDAALDTKNASLIGDMISNASKES----QFIVISHREQMISKSNVMYGVC 1186
Cdd:PRK01156 804 GGEKTAVAFALRVAVAQflNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSsdipQVIMISHHRELLSVADVAYEVK 883
|
570
....*....|..
gi 33578097 1187 MENGLSKIVSVK 1198
Cdd:PRK01156 884 KSSGSSKVIPLR 895
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
4-63 |
5.66e-09 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 59.63 E-value: 5.66e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSFKNTKLKIPDGFTAILGPNGSGKSNTIDGICFVLGKTSAKSLRAGKFNQ 63
Cdd:COG3593 3 LEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYL 62
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
4-107 |
5.81e-09 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 58.46 E-value: 5.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSFKNTKLKIPDGFTAILGPNGSGKSNTIDGICFVlgkTSAKSLRAGKFNQLITYHngkrADYAEVTLFFD 83
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLL---ATGKSHRTSRDKELIRWG----AEEAKISAVLE 73
|
90 100
....*....|....*....|....*...
gi 33578097 84 NINREIPIDsdkVGIC----RKVKLNGD 107
Cdd:cd03242 74 RQGGELALE---LTIRsgggRKARLNGI 98
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
315-947 |
7.54e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.03 E-value: 7.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 315 EEVMELHKSIKELEVNLNNDKNALENAIDDLKHTLKMEESKNNDLNETKEKINNIRIDTLKKEAEAKVLIKEIEKLNEER 394
Cdd:TIGR04523 75 NKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 395 QNLEKKVEQSESQVKALKNQESKLSERINDTQKELYGLKNELNQLENTLNNRTFDYQKNNETIENLTNQIAEFSDLEDTK 474
Cdd:TIGR04523 155 EKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNI 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 475 KL---------------YKELEDIAVELEFSKKKLQEKITERNDSQSKLDNLHSEYVKENARIKTLKDMENFSLDRAVKG 539
Cdd:TIGR04523 235 EKkqqeinektteisntQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKS 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 540 VLDAKLPGVVDIAGNLAKTKgeyktaievaggarlnhivvKKMDDGSRAINYLKQKrlgratflpmdrikgmdaKDISDT 619
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNN--------------------KIISQLNEQISQLKKE------------------LTNSES 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 620 GIIGKAIDLVEFDIKYTNVFKFIFGNTHIVDNLENAKKlSLKYKARFVTLEGEVIEpsgamvggnirrnsaIKVDIDMKK 699
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIN-DLESKIQNQEKLNQQKD---------------EQIKKLQQE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 700 LTNLSEDIKELEQILSNVKDEIERLNNKINTCSTRKLELDNRLKIARDQEFKKEEITKSNNLKIKELNMLNSKIDDEISE 779
Cdd:TIGR04523 421 KELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 780 LTDEKEILSQKVQNLDNKLSEVMGQRErivneiksyensELSKRIKEIDHKIRENESSKNTLENEIKKGAI-LVKEVLIP 858
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIE------------KLESEKKEKESKISDLEDELNKDDFELKKENLeKEIDEKNK 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 859 KISELNSNIKSLADKKNMFKNSVEIYKSNIESNSSILSDKRGKYEELTKGLKDLTDKKECYELEIENLQNNKEELREKAT 938
Cdd:TIGR04523 569 EIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
....*....
gi 33578097 939 DIDNQVNVI 947
Cdd:TIGR04523 649 QIKETIKEI 657
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
168-527 |
8.14e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.03 E-value: 8.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 168 LQGDLLRIIDTSPNERRKILDEVSGVAEFDEKSEKAKKELSQAREYIEKIDIRINEVRANLEKLKKEKEDAEKY--TVYN 245
Cdd:TIGR04523 101 LNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENElnLLEK 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 246 KKLKVTKYILTSK----KVEFLKMVLDETKDEIEALKETKNCYIQDISNIDSEIIGLKVKINELVNELNEKgseevmelH 321
Cdd:TIGR04523 181 EKLNIQKNIDKIKnkllKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNT--------Q 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 322 KSIKELEVNLNNDKNALENAIDDLKHTLKMEESKNNDLNETKEKINNiridtLKKEAEA---KVLIKEIEKLNEERQNLE 398
Cdd:TIGR04523 253 TQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD-----LNNQKEQdwnKELKSELKNQEKKLEEIQ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 399 KKVEQSESQVKALKNQESKLSERINDTQKELYGLKNELNQLENTLNNRTFDYQKNNETIENLTNQIAEF-SDLEDTKKLY 477
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLeSKIQNQEKLN 407
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 33578097 478 KELEDIAVELEFSKKKLQEKIT----ERNDSQSKLDNLHSEYVKENARIKTLKD 527
Cdd:TIGR04523 408 QQKDEQIKKLQQEKELLEKEIErlkeTIIKNNSEIKDLTNQDSVKELIIKNLDN 461
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
3-97 |
8.65e-09 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 57.22 E-value: 8.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 3 SISEIHLKNFKSFKNTKLKIPDGFTAILGPNGSGKSNTIDGICFVLGKTSAKSLRAGKFNQLItyHNGKRADYAEVTLFf 82
Cdd:cd03277 2 SIVRIKLENFVTYDETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPKLLGRAKKVGEFV--KRGCDEGTIEIELY- 78
|
90 100
....*....|....*....|..
gi 33578097 83 dNINREIPIDS-------DKVG 97
Cdd:cd03277 79 -GNPGNIQVDNlcqflpqDRVG 99
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1111-1179 |
9.45e-09 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 55.71 E-value: 9.45e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1111 MSGGEKSLTALAFLFAiqrLNPsPFYVLDEVDAALDTKNASLIGDMISNASKE-SQFIVISHREQMISKS 1179
Cdd:cd00267 81 LSGGQRQRVALARALL---LNP-DLLLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELA 146
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
4-592 |
1.01e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSFKNTKLKIPDGFTAILGPNGSGKSNTIDGICFVLGKTSAKSLRA-GKFNQLITYHNGKRADYAEVTLff 82
Cdd:COG4717 3 IKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKSTLLAFIRAMLLERLEKEADElFKPQGRKPELNLKELKELEEEL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 83 dninreipidsdkvgicrkvklngdnnyyvvwYEVEKQNTKINTESSQKKTSKASKVEKRRRMKK-NEVLDLLSKisLIA 161
Cdd:COG4717 81 --------------------------------KEAEEKEEEYAELQEELEELEEELEELEAELEElREELEKLEK--LLQ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 162 DGPNIILQGDLLRIIDTSPNERRKILDEVSGVAEFDEKSEKAKKELSQAREYIEKIDIRIN-EVRANLEKLKKEKEDA-E 239
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELqQ 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 240 KYTVYNKKLKVTKyiltsKKVEFLKMVLDETKDEIEALKE----TKNCYIQDISNIDSEIIGLKVKINELVNELNEK--- 312
Cdd:COG4717 207 RLAELEEELEEAQ-----EELEELEEELEQLENELEAAALeerlKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlfl 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 313 --GSEEVMELHKSIKELEVNLNNDKNALENAIDDLKHTLKMEESKNNDLNETKEKINNirIDTLKKEAEAKVLIKEIEKL 390
Cdd:COG4717 282 vlGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEL--LELLDRIEELQELLREAEEL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 391 NEERQNLEKKVEQSESQVKALKNQESKLSERINDTQKELyGLKNELNQLENTLNN---------RTFDYQKNNETIENLT 461
Cdd:COG4717 360 EEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEEllgeleellEALDEEELEEELEELE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 462 NQIAEFSdlEDTKKLYKELEDIAVELEF--SKKKLQEKITERNDSQSKLDnlhsEYVKENARIKTLKDMenfsLDRAVKG 539
Cdd:COG4717 439 EELEELE--EELEELREELAELEAELEQleEDGELAELLQELEELKAELR----ELAEEWAALKLALEL----LEEAREE 508
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 33578097 540 VLDAKLPGVVDIAGNLAK--TKGEYkTAIEVAGGarlNHIVVKKMDDGSRAINYL 592
Cdd:COG4717 509 YREERLPPVLERASEYFSrlTDGRY-RLIRIDED---LSLKVDTEDGRTRPVEEL 559
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
4-458 |
1.44e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 59.14 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSFKNTKLKIPDGFTAILGPNGSGKSNTIDGICFVLGKTSakslRAGKFNQLITyhngKRADYAEVTLFFD 83
Cdd:PRK01156 3 IKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTDK----RTEKIEDMIK----KGKNNLEVELEFR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 84 ninreipIDSDKVGICRKVKLNGDNNyyvvwyEVEKQNTKINTESSQKKTSKASKVEKRRRMKKNEVldLLSKIsliadg 163
Cdd:PRK01156 75 -------IGGHVYQIRRSIERRGKGS------RREAYIKKDGSIIAEGFDDTTKYIEKNILGISKDV--FLNSI------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 164 pnIILQGDLLRIIDTSPNERRKILDEVSGVAEFDEKSEKAKKELSQAREYIEKIDIRINEVR------ANLEKLKKEKED 237
Cdd:PRK01156 134 --FVGQGEMDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKssnlelENIKKQIADDEK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 238 AEKYTVYNKKLKVTKYILTSKKveflKMVLDETKDEIEALKETKNCYIQDISNIDS----------EIIGLKVKINELVN 307
Cdd:PRK01156 212 SHSITLKEIERLSIEYNNAMDD----YNNLKSALNELSSLEDMKNRYESEIKTAESdlsmeleknnYYKELEERHMKIIN 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 308 ELNEKGSEEVMELHKSIKELE------VNLNNDKNALENAIDDLKhTLKMEESKNNDLNETKEKINNIRIDTLKKEAEAK 381
Cdd:PRK01156 288 DPVYKNRNYINDYFKYKNDIEnkkqilSNIDAEINKYHAIIKKLS-VLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYN 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33578097 382 VLIKEIEKLNEERQNLEKKVEQSESQVKALKNQESKLSERINDTQKELYGLKNELNQLENTLNNRTFDYQKNNETIE 458
Cdd:PRK01156 367 SYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELS 443
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
3-106 |
1.57e-08 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 58.25 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 3 SISEIHLKNFKSFKNTKLKIPDGFTAILGPNGSGKSNTIDGIcFVLGKtsAKSLRAGKFNQLITYHngkrADYAEVTLFF 82
Cdd:PRK00064 2 YLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAI-YLLAP--GRSHRTARDKELIRFG----AEAAVIHGRV 74
|
90 100
....*....|....*....|....*
gi 33578097 83 DNINREIPIDSDKVGIC-RKVKLNG 106
Cdd:PRK00064 75 EKGGRELPLGLEIDKKGgRKVRING 99
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
161-972 |
3.56e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 58.21 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 161 ADGPNIILQGDLLRIIDTSPNERRKIL-----DEVSGV-AEFDEKSEKAKKELSQAREYIEKIDIRINEVRANLE-KLKK 233
Cdd:pfam15921 42 TSSTGTFTQIPIFPKYEVELDSPRKIIaypgkEHIERVlEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQtKLQE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 234 EKEDAEKYTVYNKKlkvtkyilTSKKVEFLKMVLDETKDEIEALKETKNCYIQDiSNIDSEII--------GLKVKINEL 305
Cdd:pfam15921 122 MQMERDAMADIRRR--------ESQSQEDLRNQLQNTVHELEAAKCLKEDMLED-SNTQIEQLrkmmlsheGVLQEIRSI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 306 VNELNEKGSEEVME-----------LHKSIKELEVNLNNDKNALENAIDDLKHTLKMEESKNNDLNETKEKINNIRIDTL 374
Cdd:pfam15921 193 LVDFEEASGKKIYEhdsmstmhfrsLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 375 KKEAEAkvlikEIEKLNEERQNLEKKVEQSESQVKAL----KNQESKLSERINDTQKELYGLKNELNQLENTLNNRTFDY 450
Cdd:pfam15921 273 ISEHEV-----EITGLTEKASSARSQANSIQSQLEIIqeqaRNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEEL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 451 QK-----NNETIENLT--NQIAEFS-DLEDT-KKLYKELEDIAVELEFSKKKlQEKITERNDSQS--------KLDNLHS 513
Cdd:pfam15921 348 EKqlvlaNSELTEARTerDQFSQESgNLDDQlQKLLADLHKREKELSLEKEQ-NKRLWDRDTGNSitidhlrrELDDRNM 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 514 EYVKENARIKTLKDMENFSLDRAVKGVL--DAKLPGVVDIAGNLAKTKGEYKTAIEvaggarlnHIVVKKM--DDGSRAI 589
Cdd:pfam15921 427 EVQRLEALLKAMKSECQGQMERQMAAIQgkNESLEKVSSLTAQLESTKEMLRKVVE--------ELTAKKMtlESSERTV 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 590 NYLkqkrlgraTFLPMDRIKGMDAKDISDTGIIGKAidlvefDIKYTNVFKFIFGNTHI--VDNLENAKKLSLKYKARFV 667
Cdd:pfam15921 499 SDL--------TASLQEKERAIEATNAEITKLRSRV------DLKLQELQHLKNEGDHLrnVQTECEALKLQMAEKDKVI 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 668 TLEGEVIEPSGAMVGGNIRRNSAIKVDIDM--KKLTNLSEDIKELeQILSNVKD-EIERLNNKINTCSTRKLELDN---- 740
Cdd:pfam15921 565 EILRQQIENMTQLVGQHGRTAGAMQVEKAQleKEINDRRLELQEF-KILKDKKDaKIRELEARVSDLELEKVKLVNagse 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 741 RLKIARDqeFKKEEITKSNNLKikelnmlNSKidDEISELTDEKEILSQkvqNLDNKLSEVMGQRERIVNEIKSYEnSEL 820
Cdd:pfam15921 644 RLRAVKD--IKQERDQLLNEVK-------TSR--NELNSLSEDYEVLKR---NFRNKSEEMETTTNKLKMQLKSAQ-SEL 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 821 skrikeidhkirenESSKNTLEN-EIKKG-AILVKEVLIPKISELNSNIKSLADKKNMFKNSVeiykSNIESNSSILSDK 898
Cdd:pfam15921 709 --------------EQTRNTLKSmEGSDGhAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAM----TNANKEKHFLKEE 770
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33578097 899 RGKyeeLTKGLKDLTDKKECYELEIENLQNNKEELREKATDIDNQVNVINVDRAKYE---TRLEEEERKLYLCDTLE 972
Cdd:pfam15921 771 KNK---LSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQdiiQRQEQESVRLKLQHTLD 844
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
193-508 |
9.24e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 9.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 193 VAEFDEKSEKAKKELSQAREYIEKiDIRINEVRANLEKLKKEKEDAEKYTVYNKKLKVTKYILTSKKVEFLKMVLDETKD 272
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKK 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 273 EIEALKETKNcyiqDISNIDSEIIGLKVKINELVNELNEKGSEEVMELHKSIKELEvNLNNDKNALENAIDDLKHTLKME 352
Cdd:PRK03918 547 ELEKLEELKK----KLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDAEKELEREEKEL 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 353 ESKNNDLNETKEKINNI--RIDTLKKEAEAKVLI---KEIEKLNEERQNLEKKVEQSESQVKALKNQESKLSERINDTQK 427
Cdd:PRK03918 622 KKLEEELDKAFEELAETekRLEELRKELEELEKKyseEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKE 701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 428 ELYGLKNELNQLENtlnnrtfdYQKNNETIENLTNQIAEFSDLEDTKKLyKELEDIAVEL--EFSKKKLQEKITERNDSQ 505
Cdd:PRK03918 702 ELEEREKAKKELEK--------LEKALERVEELREKVKKYKALLKERAL-SKVGEIASEIfeELTEGKYSGVRVKAEENK 772
|
...
gi 33578097 506 SKL 508
Cdd:PRK03918 773 VKL 775
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
181-529 |
1.02e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 181 NERRKILDEVSGVAEFDEKSEKAKKELSQAREYIEKIDIRinevraNLEKLKKEKEDAEKytvynKKLKVTKYI--LTSK 258
Cdd:PRK03918 345 KKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGL------TPEKLEKELEELEK-----AKEEIEEEIskITAR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 259 KVEfLKMVLDETKDEIEALKETK-------------------NCYIQDISNIDSEIIGLKVKINELVNELNE-----KGS 314
Cdd:PRK03918 414 IGE-LKKEIKELKKAIEELKKAKgkcpvcgrelteehrkellEEYTAELKRIEKELKEIEEKERKLRKELRElekvlKKE 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 315 EEVMELHKSIKELEvnlnndknALENAIDdlKHTLKMEESKNNDLNETKEKINNIR--IDTLKKEAEA--------KVLI 384
Cdd:PRK03918 493 SELIKLKELAEQLK--------ELEEKLK--KYNLEELEKKAEEYEKLKEKLIKLKgeIKSLKKELEKleelkkklAELE 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 385 KEIEKLNEERQNLEKKVEqsESQVKALKNQESKLSE---------RINDTQKELYGLKNELNQLENTLNNRTFDYQKNNE 455
Cdd:PRK03918 563 KKLDELEEELAELLKELE--ELGFESVEELEERLKElepfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEK 640
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33578097 456 TIENLTNQIAEFS---DLEDTKKLYKELEDIAVELEFSKKKLQEKITERNDSQSKLDNLHSEYVKENARIKTLKDME 529
Cdd:PRK03918 641 RLEELRKELEELEkkySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1096-1170 |
2.43e-07 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 52.60 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1096 IDASPMNKQLQ---------------NLDVMSGGEKSLTALAFLFAIQRLNPSPFYVLDEVDAALDTKNASLIGDMISNA 1160
Cdd:cd03276 80 LDANPLCVLSQdmarsfltsnkaavrDVKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKE 159
|
90
....*....|...
gi 33578097 1161 SKES---QFIVIS 1170
Cdd:cd03276 160 AKKQpgrQFIFIT 172
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
6-59 |
2.69e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 51.59 E-value: 2.69e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 33578097 6 EIHLKNFKS-FKNTKLKIPDG-FTAILGPNGSGKSNTIDGICFVLGKTSAKSLRAG 59
Cdd:cd03227 1 KIVLGRFPSyFVPNDVTFGEGsLTIITGPNGSGKSTILDAIGLALGGAQSATRRRS 56
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
249-867 |
3.56e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 249 KVTKYILTSKKVEFLKMVLDETKDEIEALKETKNCYIQDISNIDSEIIGLKVKINELVNELNEKGSEevmelhksikele 328
Cdd:PRK03918 149 KVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSE------------- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 329 vnlnndknalenaIDDLKHTLKMEESKNNDLNETKEKINNIRIDTLKKEAEAKVLIKEIEKLNEERQNLEKKVEQSESQV 408
Cdd:PRK03918 216 -------------LPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 409 KALKNQESKLSERIndtqkELYGLKNELNQLENTLNNRTFDYQKNNETIEnltnqiAEFSDLEDTKKLYKELEDIAVELE 488
Cdd:PRK03918 283 KELKELKEKAEEYI-----KLSEFYEEYLDELREIEKRLSRLEEEINGIE------ERIKELEEKEERLEELKKKLKELE 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 489 FSKKKLQEKITERNDSQSKLDNLhsEYVKENARIKTLKDMEN-FSLDRAVKGVLDAKLPGVVDIAGNLAKTKGEYKTAIE 567
Cdd:PRK03918 352 KRLEELEERHELYEEAKAKKEEL--ERLKKRLTGLTPEKLEKeLEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 568 VAGGARLNHIVVKKMDDGSRAINYLKQKRLGRATFLP-MDRIKGMDAKDISDTGIIGKAIDLVEFDIKYTNVFKFIFG-- 644
Cdd:PRK03918 430 ELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKeLKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKEle 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 645 ---NTHIVDNLENAKKLSLKYKARFVTLEGEVIepsgaMVGGNIRRNSAIKvdidmKKLTNLSEDIKELEQILSNVKDEI 721
Cdd:PRK03918 510 eklKKYNLEELEKKAEEYEKLKEKLIKLKGEIK-----SLKKELEKLEELK-----KKLAELEKKLDELEEELAELLKEL 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 722 ERLN------------------NKINTCSTRKLELDNRLKIARDQEFKKEEITKSNNLKIKELNMLNSKIDDEISELTDE 783
Cdd:PRK03918 580 EELGfesveeleerlkelepfyNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 784 K-EILSQKVQNLDNKLSEVMGQRERIVNEIKSYENS--ELSKRIKEIDHKIRENESSKNTLEN------EIKKGAILVKE 854
Cdd:PRK03918 660 EyEELREEYLELSRELAGLRAELEELEKRREEIKKTleKLKEELEEREKAKKELEKLEKALERveelreKVKKYKALLKE 739
|
650
....*....|...
gi 33578097 855 VLIPKISELNSNI 867
Cdd:PRK03918 740 RALSKVGEIASEI 752
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
4-83 |
3.78e-07 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 53.08 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSFKNTK--LKIPDGFTAILGPNGSGKSNTIDGICFVLGkTSAKSLRAGKFNQLITyHNGKRADYAEVTLF 81
Cdd:COG3950 3 IKSLTIENFRGFEDLEidFDNPPRLTVLVGENGSGKTTLLEAIALALS-GLLSRLDDVKFRKLLI-RNGEFGDSAKLILY 80
|
..
gi 33578097 82 FD 83
Cdd:COG3950 81 YG 82
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
267-466 |
4.35e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 267 LDETKDEIEAL-------KETKNCYIQDISNIDSEIIGLKVKINELVNELNEKgSEEVMELHKSIKELEVNLNNDKNALE 339
Cdd:COG4942 29 LEQLQQEIAELekelaalKKEEKALLKQLAALERRIAALARRIRALEQELAAL-EAELAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 340 NAIDDL----KHTLKMEESKNNDLNETKEKINNIRIDTLKKEAEAKVLIKEIEKLNEERQNLEKKVEQSESQVKALKNQE 415
Cdd:COG4942 108 ELLRALyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEER 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 33578097 416 SKLSERINDTQKELYGLKNELNQLENTLNNRTFDYQKNNETIENLTNQIAE 466
Cdd:COG4942 188 AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
1095-1180 |
5.27e-07 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 52.59 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1095 LIDASPMNKQLQNLDVMSGGEKSLTALAFLFAIQRLNPSPFYVLDEVDAALDTKNASLIGDMISNASKESQFIVISHREQ 1174
Cdd:cd03241 155 LFSTNPGEPLKPLAKIASGGELSRLMLALKAILARKDAVPTLIFDEIDTGISGEVAQAVGKKLKELSRSHQVLCITHLPQ 234
|
....*.
gi 33578097 1175 MISKSN 1180
Cdd:cd03241 235 VAAMAD 240
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1110-1190 |
5.68e-07 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 50.84 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1110 VMSGGEKSLTALAflfaiqR--LNPSPFYVLDEVDAALDTKNASLIGDMISNASKESQFIVISHREQMISKSNVMYgvCM 1187
Cdd:cd03228 96 ILSGGQRQRIAIA------RalLRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRII--VL 167
|
...
gi 33578097 1188 ENG 1190
Cdd:cd03228 168 DDG 170
|
|
| recN |
TIGR00634 |
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ... |
819-1174 |
6.75e-07 |
|
DNA repair protein RecN; All proteins in this family for which functions are known are ATP binding proteins involved in the initiation of recombination and recombinational repair. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273187 [Multi-domain] Cd Length: 563 Bit Score: 53.58 E-value: 6.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 819 ELSKRIKEIDHKIRENESSKNTLE---NEIKKGAILVKEVLipkiselnsnikSLADKKNMFKNSVEIYKSNIESNSSIL 895
Cdd:TIGR00634 172 KARQQLKDRQQKEQELAQRLDFLQfqlEELEEADLQPGEDE------------ALEAEQQRLSNLEKLRELSQNALAALR 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 896 SDK----RGKYEELTKGLKDL-TDKKECYELEIENLQNNKEELREKATDIDNQVNVINVDrakyETRLEEEERKLYLCDT 970
Cdd:TIGR00634 240 GDVdvqeGSLLEGLGEAQLALaSVIDGSLRELAEQVGNALTEVEEATRELQNYLDELEFD----PERLNEIEERLAQIKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 971 LEniedisdemieETYSLEIDDLERNQAllessikklepvnmRAIEDYDFINERYEELFGKRKEYEQEEGKYLQLISEVQ 1050
Cdd:TIGR00634 316 LK-----------RKYGASVEEVLEYAE--------------KIKEELDQLDDSDESLEALEEEVDKLEEELDKAAVALS 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1051 KRKKETFMKTYDRVAENYEQIYGEiggNGKLSLENEEDPFSGGLL------ID------ASPMNKQLQNL-DVMSGGEKS 1117
Cdd:TIGR00634 371 LIRRKAAERLAKRVEQELKALAME---KAEFTVEIKTSLPSGAKAragaygADqveflfSANTGEPVKPLaKVASGGELS 447
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 33578097 1118 LTALAFLFAIQRLNPSPFYVLDEVDAALDTKNASLIGDMISNASKESQFIVISHREQ 1174
Cdd:TIGR00634 448 RVMLALKVVLSSSAAVTTLIFDEVDVGVSGETAQAIAKKLAQLSERHQVLCVTHLPQ 504
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
286-512 |
6.82e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.48 E-value: 6.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 286 QDISNIDSEIIGLKVKI---NELVNELNEKGSEEVMELHKSIKELEVNLNNDKNALENAIDDLKHTLKMEESKNNDLNet 362
Cdd:PHA02562 181 QQIQTLDMKIDHIQQQIktyNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALN-- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 363 keKINNIRIdtlKKEAEAKVLIKEIEKLNEE------RQNLEKKVEQSESQVKALKNQESKLsERINDTQKELYGLKNEL 436
Cdd:PHA02562 259 --KLNTAAA---KIKSKIEQFQKVIKMYEKGgvcptcTQQISEGPDRITKIKDKLKELQHSL-EKLDTAIDELEEIMDEF 332
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33578097 437 NQLENTLNNRTFDYQKNNETIENLTNQIaefSDLEDT-KKLYKELEDIAVELEFSKKKLQEKITERNDSQSKLDNLH 512
Cdd:PHA02562 333 NEQSKKLLELKNKISTNKQSLITLVDKA---KKVKAAiEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRG 406
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
330-562 |
8.16e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 8.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 330 NLNNDKNALENAIDDLKHTLKMEESKNNDLNETKEKINNiRIDTLkkEAEAKVLIKEIEKLNEERQNLEKKVEQSEsqvK 409
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-RIAAL--ARRIRALEQELAALEAELAELEKEIAELR---A 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 410 ALKNQESKLSERINDTQK--ELYGLKNELNQLENTLNNRTFDY-----QKNNETIENLTNQIAEFSDLEDT-KKLYKELE 481
Cdd:COG4942 98 ELEAQKEELAELLRALYRlgRQPPLALLLSPEDFLDAVRRLQYlkylaPARREQAEELRADLAELAALRAElEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 482 DIAVELEFSKKKLQEKITERndsQSKLDNLHSEYVKENARIKTLKDMENfSLDRAVKGVL-DAKLPGVVDIAGNLAKTKG 560
Cdd:COG4942 178 ALLAELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEAE-ELEALIARLEaEAAAAAERTPAAGFAALKG 253
|
..
gi 33578097 561 EY 562
Cdd:COG4942 254 KL 255
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
7-234 |
8.90e-07 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 50.57 E-value: 8.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 7 IHLKNFKSFKNTKLKIPDGFTAILGPNGSGKSNTIDGICFVLGKTSAKSLRAGKFNQLItyhngkradyAEVTLFFDNIN 86
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVK----------GDIRIGLEGKG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 87 REipidsdkvgiCRKVKLNGDNNYYVVWYEVEKQNTKINTESSQKKTSKASKVEKRRRMKKNEVLDLLSKISLIAdgpnI 166
Cdd:pfam13476 71 KA----------YVEITFENNDGRYTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLV----F 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33578097 167 ILQGDLLRIIDTSPNERRKILdevsgvaefdeksEKAKKELSQAREYIEKIdIRINEVRANLEKLKKE 234
Cdd:pfam13476 137 LGQEREEEFERKEKKERLEEL-------------EKALEEKEDEKKLLEKL-LQLKEKKKELEELKEE 190
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
4-112 |
8.90e-07 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 51.49 E-value: 8.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSFKNTKlkIPDGFT----AILGPNGSGKSNTIDGICFVLGKtSAKSLRAGKFNQLITYHNGKRADYAEVT 79
Cdd:cd03272 1 IKQVIIQGFKSYKDQT--VIEPFSpkhnVVVGRNGSGKSNFFAAIRFVLSD-EYTHLREEQRQALLHEGSGPSVMSAYVE 77
|
90 100 110
....*....|....*....|....*....|...
gi 33578097 80 LFFDNINREIPIDSDKVGICRKVKLNGDnNYYV 112
Cdd:cd03272 78 IIFDNSDNRFPIDKEEVRLRRTIGLKKD-EYFL 109
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
197-429 |
9.30e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 9.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 197 DEKSEKAKKELSQAREYIEKIDIRINEVRANLEKLKKEKEDAEKytvynkklkvtkyiltskkveflkmVLDETKDEIEA 276
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA-------------------------ELEALQAEIDK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 277 LKEtkncyiqDISNIDSEIIGLKVKINELVNELNEKGSeevmelhkSIKELEVNLNNDknALENAIDDLKHTLKMEESKN 356
Cdd:COG3883 70 LQA-------EIAEAEAEIEERREELGERARALYRSGG--------SVSYLDVLLGSE--SFSDFLDRLSALSKIADADA 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33578097 357 NDLNETKEKINniRIDTLKKEAEAKV--LIKEIEKLNEERQNLEKKVEQSESQVKALKNQESKLSERINDTQKEL 429
Cdd:COG3883 133 DLLEELKADKA--ELEAKKAELEAKLaeLEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
135-826 |
1.00e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.20 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 135 KASKVEKRRRMK-KNEVLDLLSKISLIADGpniILQGDLLRIIDTSPNERRKILDEVS-GVAEFDEKSEKAKKELSQARE 212
Cdd:pfam15921 155 EAAKCLKEDMLEdSNTQIEQLRKMMLSHEG---VLQEIRSILVDFEEASGKKIYEHDSmSTMHFRSLGSAISKILRELDT 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 213 YIEKIDIRINEVRANLEKLKKEKEDAEKytvynkklkvtkyILTSKKVEFLKMVLDETKDEIEALKETKNCYIQDISNID 292
Cdd:pfam15921 232 EISYLKGRIFPVEDQLEALKSESQNKIE-------------LLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQ 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 293 SEiigLKVkINELVNELNEKGSEEVMELHKSIKELEVNLNNDKNALENAIDDLKHTLKMeesKNNDLNETKEKINNIrid 372
Cdd:pfam15921 299 SQ---LEI-IQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVL---ANSELTEARTERDQF--- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 373 tlkkEAEAKVLIKEIEKLNEERQNLEKKVEQSESQVKALKNQESKLSERINDTQKELYGLKNELNQLENTLN-------- 444
Cdd:pfam15921 369 ----SQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKamksecqg 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 445 ---NRTFDYQKNNETIENLTNQIAEF-SDLEDTKKLYKELEDIAVELEFSKKKLQEKITERNDSQSKLDNLHSEYVKENA 520
Cdd:pfam15921 445 qmeRQMAAIQGKNESLEKVSSLTAQLeSTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRS 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 521 RIktlkdmenfsldravkgvlDAKLPGVVDIagnlaKTKGEYKTAIEVAGGArlnhiVVKKMDDGSRAINYLKQK----- 595
Cdd:pfam15921 525 RV-------------------DLKLQELQHL-----KNEGDHLRNVQTECEA-----LKLQMAEKDKVIEILRQQienmt 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 596 ----RLGRaTFLPMDRIKGMDAKDISDtgiigKAIDLVEFdikytnvfkfifgntHIVDNLENAKKLSLkyKARFVTLEG 671
Cdd:pfam15921 576 qlvgQHGR-TAGAMQVEKAQLEKEIND-----RRLELQEF---------------KILKDKKDAKIREL--EARVSDLEL 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 672 EVIEpsgaMVGGNIRRNSAIKvDIDMKK-------------LTNLSEDIKELEQILSNVKDEIERLNNKIN-TCSTRKLE 737
Cdd:pfam15921 633 EKVK----LVNAGSERLRAVK-DIKQERdqllnevktsrneLNSLSEDYEVLKRNFRNKSEEMETTTNKLKmQLKSAQSE 707
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 738 LD---NRLKIARDQEFKKEEIT----KSNNLKIKELNMLNSKI---DDEISELTDEKEILSQKVQNLDNKLSEVMGQRER 807
Cdd:pfam15921 708 LEqtrNTLKSMEGSDGHAMKVAmgmqKQITAKRGQIDALQSKIqflEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNK 787
|
730
....*....|....*....
gi 33578097 808 IVNEIKSYENSElsKRIKE 826
Cdd:pfam15921 788 MAGELEVLRSQE--RRLKE 804
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
9-514 |
1.13e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.05 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 9 LKNFKSFKNTKL---KIPDGFTAILGPNGSGKSNTIDGICFVL-GKTSakslRAGKFNQLITYHNGKRADYAEVTLffdn 84
Cdd:TIGR00618 8 LKNFGSYKGTHTidfTALGPIFLICGKTGAGKTTLLDAITYALyGKLP----RRSEVIRSLNSLYAAPSEAAFAEL---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 85 inreipidsdkvgicrKVKLNGDNnYYVVWYEVEKQNTKINTESSQKKTSKASKVEKRRRMKKNEVLDLLSKISLIADGP 164
Cdd:TIGR00618 80 ----------------EFSLGTKI-YRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 165 --NIIL--QGDLLRIIDTSPNERRKILDEVSGVAEFDE---------KSEKAKKELSQAREYIEKIDI-----RINEVRA 226
Cdd:TIGR00618 143 ftRVVLlpQGEFAQFLKAKSKEKKELLMNLFPLDQYTQlalmefakkKSLHGKAELLTLRSQLLTLCTpcmpdTYHERKQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 227 NLEKLKKEKEDA---EKYTVYNKKLKVTKYILTSKKVEFLKMVLDETKD------EIEALKETKN--CYIQDISNIDSEI 295
Cdd:TIGR00618 223 VLEKELKHLREAlqqTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEElraqeaVLEETQERINraRKAAPLAAHIKAV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 296 IGLKVKINELVNELNEKGSEEVMELHKsikelEVNLNNDKNALENAiDDLKHTLKMEESKNNDLNETKEKINNIRIDTLK 375
Cdd:TIGR00618 303 TQIEQQAQRIHTELQSKMRSRAKLLMK-----RAAHVKQQSSIEEQ-RRLLQTLHSQEIHIRDAHEVATSIREISCQQHT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 376 KEAEAKVLIKEIEKLNEERQNLEKKVEQSESQVkalKNQESKLSERINDTQKELYGLKNELNQLENTLNNRTFdyqknne 455
Cdd:TIGR00618 377 LTQHIHTLQQQKTTLTQKLQSLCKELDILQREQ---ATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAA------- 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 33578097 456 TIENLTNQIAEFSDLEDTKKLYKELEdiavELEFSKKKLQEKITERNDSQSKLDNLHSE 514
Cdd:TIGR00618 447 ITCTAQCEKLEKIHLQESAQSLKERE----QQLQTKEQIHLQETRKKAVVLARLLELQE 501
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
707-847 |
1.19e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.08 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 707 IKELEQILSNVKDEIERLNNKINTCSTRKLELDNRLKIARDQEFKKEEITKSNNLKIKELN--MLNSKIDDEISELTDEK 784
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqLGNVRNNKEYEALQKEI 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33578097 785 EILSQKVQNLDNKLSEVMGQRERIVNEIKSYEnSELSKRIKEIDHKIRENESSKNTLENEIKK 847
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELE-AELAELEAELEEKKAELDEELAELEAELEE 160
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
859-1178 |
1.37e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 52.32 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 859 KISELNSNIKSLADKKNMFKNSVEIYKSNIES----NSSILSDKRGKYEELTKGLKD-------LTDKKECYELEIENLQ 927
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEqrkkNGENIARKQNKYDELVEEAKTikaeieeLTDELLNLVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 928 NNKEELREKATDIDNQVNVINVDRAKYETRLEEEERKLYLCDTLENIEDISDEMIEETYSLE-----IDDL-ERNQALLE 1001
Cdd:PHA02562 255 AALNKLNTAAAKIKSKIEQFQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEkldtaIDELeEIMDEFNE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1002 SSIKKLEPVNMRAIEDYDFINERYEELFGKR--KEYEQEEGKYLQLISEVQKRKKETFMKTYDRVAENYEQ--IYGEIGG 1077
Cdd:PHA02562 335 QSKKLLELKNKISTNKQSLITLVDKAKKVKAaiEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRgiVTDLLKD 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1078 NG-KLSLENEEDPFsggllidaspMNKQL-QNLDVM-----------------------------SGGEKSLTALAFLFA 1126
Cdd:PHA02562 415 SGiKASIIKKYIPY----------FNKQInHYLQIMeadynftldeefnetiksrgredfsyasfSQGEKARIDLALLFT 484
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 33578097 1127 ---IQRLNPS---PFYVLDEV-DAALDTKNASLIGDMISNAsKESQFIVISHREQMISK 1178
Cdd:PHA02562 485 wrdVASKVSGvdtNLLILDEVfDGALDAEGTKALLSILDSL-KDTNVFVISHKDHDPQK 542
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
287-444 |
1.62e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 287 DISNIDSEIIGLKVKINELVNELNEkgseevmelhksIKELEVNLNNDKNALENAIDDLKHTLKMEESKNNDLNETKEKI 366
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAE------------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33578097 367 NNiRIDTLKKEAEAKVLIKEIEKLNEERQNLEKKVEQSESQVKALKNQESKLSERINDTQKELYGLKNELNQLENTLN 444
Cdd:COG1579 79 EE-QLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
4-107 |
2.13e-06 |
|
recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273173 [Multi-domain] Cd Length: 365 Bit Score: 51.20 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSFKNTKLKIPDGFTAILGPNGSGKSNTIDGICFVlgkTSAKSLRAGKFNQLITYHngkrADYAEVTLFFD 83
Cdd:TIGR00611 3 LSRLELTDFRNYDAVDLELSPGVNVIVGPNGQGKTNLLEAIYYL---ALGRSHRTSRDKPLIRFG----AEAFVIEGRVS 75
|
90 100
....*....|....*....|....*...
gi 33578097 84 NINREIPIDS----DKVGicRKVKLNGD 107
Cdd:TIGR00611 76 KGDREVTIPLegllKKKG--KKAKVNID 101
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
4-112 |
2.49e-06 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 50.66 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSFKNTKLKIPDGFTAILGPNGSGKSNTIDGICFVLG-KTSAKSLRAGkfnqlityhngkrADYAEVTLFF 82
Cdd:cd03241 1 LLELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSLLLGgRASADLIRSG-------------AEKAVVEGVF 67
|
90 100 110
....*....|....*....|....*....|....*....
gi 33578097 83 DN---------INREIPIDSDKVGICRKVKLNGDNNYYV 112
Cdd:cd03241 68 DIsdeeeakalLLELGIEDDDDLIIRREISRKGRSRYFI 106
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
4-445 |
2.49e-06 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 51.66 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIH-LKNFKSFKN-TKLKIPDGFTAILGPNGSGKSntidGICFVLGKTSAKSLrAGKFNQLITYHNGKRA-------- 73
Cdd:COG4694 2 ITKIKkLKNVGAFKDfGWLAFFKKLNLIYGENGSGKS----TLSRILRSLELGDT-SSEVIAEFEIEAGGSApnpsvrvf 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 74 --DYAEVTLFFD-NINREIPIDSDKVGICRKV-KLNGDNNyyvvwyEVEKQNTKINTESSQKKTSKASKVEKRRRMKKNE 149
Cdd:COG4694 77 nrDFVEENLRSGeEIKGIFTLGEENIELEEEIeELEKEIE------DLKKELDKLEKELKEAKKALEKLLEDLAKSIKDD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 150 VLDLLSKISLIADGPNiiLQGDLLRIIDTSPNERRKILDEVSGVAEFDEKSEKAKKELSQAREYIEKI--DIRINEVRAN 227
Cdd:COG4694 151 LKKLFASSGRNYRKAN--LEKKLSALKSSSEDELKEKLKLLKEEEPEPIAPITPLPDLKALLSEAETLleKSAVSSAIEE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 228 LEKLKKEKEDAE------KYTVYNK------------KLKVTKYiltskkVEFLKMVLDETKDEIEALKETKNCYIQDIS 289
Cdd:COG4694 229 LAALIQNPGNSDwveqglAYHKEEEddtcpfcqqelaAERIEAL------EAYFDDEYEKLLAALKDLLEELESAINALS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 290 NIDSEII-----GLKVKINELVNELNEKGSEEVMELHKSIKELEVNLNNDKNALENAIDDLKhtlkmeesknNDLNETKE 364
Cdd:COG4694 303 ALLLEILrtllpSAKEDLKAALEALNALLETLLAALEEKIANPSTSIDLDDQELLDELNDLI----------AALNALIE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 365 KINNI--RIDTLKKEAEAKVLIKEIEKLNEERQNLEKKVEQSESQVKALKNQESKLSErINDTQKELYGLKNELNQLENT 442
Cdd:COG4694 373 EHNAKiaNLKAEKEEARKKLEAHELAELKEDLSRYKAEVEELIEELKTIKALKKALED-LKTEISELEAELSSVDEAADE 451
|
...
gi 33578097 443 LNN 445
Cdd:COG4694 452 INE 454
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
366-836 |
2.50e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 366 INNIRIDTLKKEAEA---------KVLIKEIEKLNEERQNLEKKVEQsesqVKALKNQESKLSERINDTQKELYGLKNEL 436
Cdd:COG4717 43 IRAMLLERLEKEADElfkpqgrkpELNLKELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 437 NQLEntlnnrtfdyqknnetienltNQIAEFSDLEDTKKLYKELEDIAVELEfskkKLQEKITERNDSQSKLDNLHSEYV 516
Cdd:COG4717 119 EKLE---------------------KLLQLLPLYQELEALEAELAELPERLE----ELEERLEELRELEEELEELEAELA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 517 KENARIKTLKDMENFSLDRAVKGVLDAklpgvvdiAGNLAKTKGEYKTAIEVAgGARLNHI--VVKKMDDGSRAINYLKQ 594
Cdd:COG4717 174 ELQEELEELLEQLSLATEEELQDLAEE--------LEELQQRLAELEEELEEA-QEELEELeeELEQLENELEAAALEER 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 595 KRLGRATFLPMDRIkgmdakdisdTGIIGKAIDLVEFDIKYTNVFKFIFGNTHIVDNLENAKKLSLKYKARFVTLEGEVI 674
Cdd:COG4717 245 LKEARLLLLIAAAL----------LALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 675 EPSGAMVgGNIRRNSAIKVDIDMKKLTNLSEDIKELEQILSNVKDEIERLNNKINTCSTRKL----------ELDNRLKI 744
Cdd:COG4717 315 ELEEEEL-EELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALlaeagvedeeELRAALEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 745 ARDQEFKKEEITKSN---NLKIKELNMLNSKIDDEisELTDEKEILSQKVQNLDNKLSEVMGQRERIVNEIKSYENS-EL 820
Cdd:COG4717 394 AEEYQELKEELEELEeqlEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELEQLEEDgEL 471
|
490
....*....|....*.
gi 33578097 821 SKRIKEIDHKIRENES 836
Cdd:COG4717 472 AELLQELEELKAELRE 487
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
116-527 |
3.84e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 116 EVEKQNTKINTESSQKKTSKASKVEKrrrmkKNEVLDLLSKISLIADGPNIILQgdLLRIIDTSPNERRKILDEVSgvaE 195
Cdd:TIGR04523 153 ELEKLNNKYNDLKKQKEELENELNLL-----EKEKLNIQKNIDKIKNKLLKLEL--LLSNLKKKIQKNKSLESQIS---E 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 196 FDEKSEKAKKELSQAREYIEKIDIRINEVRANLEKLKKEKEDAEKyTVYNKKLKVTKyilTSKKVEFLKMVLDETKDEIE 275
Cdd:TIGR04523 223 LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK-QLSEKQKELEQ---NNKKIKELEKQLNQLKSEIS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 276 ALKETKNCYI-----QDISNIDSEIIGLKVKI---NELVNELNEkgseEVMELHKSIKELEVNLNNDKNALENAIDDLKH 347
Cdd:TIGR04523 299 DLNNQKEQDWnkelkSELKNQEKKLEEIQNQIsqnNKIISQLNE----QISQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 348 TLKMEESKNNDLNETKEKINNIRIDTLKKEAEAKVLIKEIEKLNEERQNLEKKVEQSESQVKALKNQESKLSERINDTQK 427
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 428 ELYGLKNELNQLENTLNNRTFDYQKNNETIENLTNQiaefsdLEDTKKLYKELEDIAVELEFSKKKLQEKITErndSQSK 507
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE------LKSKEKELKKLNEEKKELEEKVKDLTKKISS---LKEK 525
|
410 420
....*....|....*....|
gi 33578097 508 LDNLHSEYVKENARIKTLKD 527
Cdd:TIGR04523 526 IEKLESEKKEKESKISDLED 545
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
697-1199 |
4.29e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 697 MKKLTNLSEDIKELEQILSNVKDEIERLNNKINTCSTRKLELDnrlkiardqEFKKEEITKSNNLKIKELNMLNSKIDDE 776
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT---------EEHRKELLEEYTAELKRIEKELKEIEEK 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 777 ISELTDEKEilsqKVQNLDNKLSEVMGQRErIVNEIKSYENSELSKRIKEIDHKIRENESSK---NTLENEIK--KGAIL 851
Cdd:PRK03918 475 ERKLRKELR----ELEKVLKKESELIKLKE-LAEQLKELEEKLKKYNLEELEKKAEEYEKLKeklIKLKGEIKslKKELE 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 852 VKEVLIPKISELNSNIKSLADKKNmfknsvEIYKSNIESNSSILSDKRGKYEELTKGLKDLTDKKECyELEIENLQNNKE 931
Cdd:PRK03918 550 KLEELKKKLAELEKKLDELEEELA------ELLKELEELGFESVEELEERLKELEPFYNEYLELKDA-EKELEREEKELK 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 932 ELREKATDIDNQVNVINVDRAKYETRLEEEERKLylcdTLENIEDISDEMIEetysleiddLERNQALLESSIKKLEPVN 1011
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRLEELRKELEELEKKY----SEEEYEELREEYLE---------LSRELAGLRAELEELEKRR 689
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1012 MRAIEDYDFINERYEELFGKRKEYEQEEgKYLQLISEVQKRKKETFMKTYDRVAENYEQIYGEI------GGNGKLSLEN 1085
Cdd:PRK03918 690 EEIKKTLEKLKEELEEREKAKKELEKLE-KALERVEELREKVKKYKALLKERALSKVGEIASEIfeelteGKYSGVRVKA 768
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1086 EEDPFSGGLLIDAspmnkQLQNLDVMSGGEKSLTALAFLFAIQ--RLNPSPFYVLDEVDAALD-TKNASLIGDMISNASK 1162
Cdd:PRK03918 769 EENKVKLFVVYQG-----KERPLTFLSGGERIALGLAFRLALSlyLAGNIPLLILDEPTPFLDeERRRKLVDIMERYLRK 843
|
490 500 510
....*....|....*....|....*....|....*..
gi 33578097 1163 ESQFIVISHREQMISKSNVMYGVCMENGLSKIVSVKL 1199
Cdd:PRK03918 844 IPQVIIVSHDEELKDAADYVIRVSLEGGVSKVEVVSL 880
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
202-501 |
5.34e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 50.60 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 202 KAKKELSQAREYIEKIDIRINEVRANLEKLKK-EKEDAEKYTVYNKKL-KVTKYILT-----SKKVEFLKMVLDETKDEI 274
Cdd:PRK04778 102 KAKHEINEIESLLDLIEEDIEQILEELQELLEsEEKNREEVEQLKDLYrELRKSLLAnrfsfGPALDELEKQLENLEEEF 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 275 ---EALKETKNcYIQD---ISNIDSEIIGLKVKINE---LVNELNEKGSEEVMELHKSIKELEV-NLNNDKNALENAIDD 344
Cdd:PRK04778 182 sqfVELTESGD-YVEAreiLDQLEEELAALEQIMEEipeLLKELQTELPDQLQELKAGYRELVEeGYHLDHLDIEKEIQD 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 345 LKHTLK--MEESKNNDLNETKEKINNI--RIDTL----KKEAEAKvliKEIEKLNEErqnLEKKVEQSESQVKALKNQES 416
Cdd:PRK04778 261 LKEQIDenLALLEELDLDEAEEKNEEIqeRIDQLydilEREVKAR---KYVEKNSDT---LPDFLEHAKEQNKELKEEID 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 417 KLSE--RINDTQKELY-GLKNELNQLENTLnnrtfdyqknNETIENLTNQIAEFSDLEDT-KKLYKELEDIavelefskK 492
Cdd:PRK04778 335 RVKQsyTLNESELESVrQLEKQLESLEKQY----------DEITERIAEQEIAYSELQEElEEILKQLEEI--------E 396
|
....*....
gi 33578097 493 KLQEKITER 501
Cdd:PRK04778 397 KEQEKLSEM 405
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
911-1171 |
5.87e-06 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 49.70 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 911 DLTDKKECYELEIENLQNNKEELREKATDIDNQVNvinvdRAKYETRLEEEERKLYLCDTLENIEDISDEmIEETYSLEI 990
Cdd:pfam13304 50 NGIDPKEPIEFEISEFLEDGVRYRYGLDLEREDVE-----EKLSSKPTLLEKRLLLREDSEEREPKFPPE-AEELRLGLD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 991 DDLERNQALLESSIKKLEPVNMRAIEDYDFINERYEELFGKRKEYEQEEGKYLQLISEVQKRKKetfmkTYDRVAENYEQ 1070
Cdd:pfam13304 124 VEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQR-----LVRGLKLADLN 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1071 IYGEIGGNGKLSLENeeDPFSGGLLIDASPMNKQLQNLDVMSGGEKSLTALAFLFaIQRLNPSPFYVLDEVDAALDTKNA 1150
Cdd:pfam13304 199 LSDLGEGIEKSLLVD--DRLRERGLILLENGGGGELPAFELSDGTKRLLALLAAL-LSALPKGGLLLIDEPESGLHPKLL 275
|
250 260
....*....|....*....|..
gi 33578097 1151 SLIGDMISNASKE-SQFIVISH 1171
Cdd:pfam13304 276 RRLLELLKELSRNgAQLILTTH 297
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
195-465 |
6.58e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 50.68 E-value: 6.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 195 EFDEKSEKAKKELSQAREYIEKIDIRINEVRANLEKLKKEKEDaekytvynkklkVTKYILTSKKVEFLKMVLDETKDEI 274
Cdd:PRK11281 70 ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDE------------ETRETLSTLSLRQLESRLAQTLDQL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 275 EALKEtkncyiqDISNIDSEIIGLkvkinelvNELNEKGSEEVMELHKSIKELEVNLNNDKNALENAIDDLKHTLKMEES 354
Cdd:PRK11281 138 QNAQN-------DLAEYNSQLVSL--------QTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 355 ---KNNDLNETKEKINNIRIDTLKKEAEAKVLikEIEKLNEERQNL-----EKKVEQSESQVKALKNQES---------- 416
Cdd:PRK11281 203 llnAQNDLQRKSLEGNTQLQDLLQKQRDYLTA--RIQRLEHQLQLLqeainSKRLTLSEKTVQEAQSQDEaariqanplv 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 417 --------KLSER-INDTQKelyglKNEL--------NQLEN-TLNNRTFDYQKN---------------------NETI 457
Cdd:PRK11281 281 aqeleinlQLSQRlLKATEK-----LNTLtqqnlrvkNWLDRlTQSERNIKEQISvlkgslllsrilyqqqqalpsADLI 355
|
....*...
gi 33578097 458 ENLTNQIA 465
Cdd:PRK11281 356 EGLADRIA 363
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
697-1055 |
7.20e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 7.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 697 MKKLTNLSEDIKELEQILSNVKDEIERLNNKINTCSTrklELDNRLKIARDQEFKKEEITKSnNLKIKELNMLNSKIDDE 776
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREINEISSELPELRE---ELEKLEKEVKELEELKEEIEEL-EKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 777 ISELTDEKEILSQKVQNLDNKLSEVmgqrERIVNEIKSYEnsELSKRIKEIDHKIRENESSKNTLENEIKKGAILVKEV- 855
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKEL----KELKEKAEEYI--KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELe 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 856 -LIPKISELNSNIKSLADKKNMFKNSVEIYKS--NIESNSSILSDKRGKY--EELTKGLKDLTDKKECYELEIENLQNNK 930
Cdd:PRK03918 335 eKEERLEELKKKLKELEKRLEELEERHELYEEakAKKEELERLKKRLTGLtpEKLEKELEELEKAKEEIEEEISKITARI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 931 EELREKATDIDNQVNVINVDRAKYET---RLEEEERKLYLCDTLENIEDISDEMIEETYSLEidDLERNQALLESSIKKl 1007
Cdd:PRK03918 415 GELKKEIKELKKAIEELKKAKGKCPVcgrELTEEHRKELLEEYTAELKRIEKELKEIEEKER--KLRKELRELEKVLKK- 491
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 33578097 1008 EPVNMRAIEDYDFINERYEELFG--------KRKEYEQEEGKYLQLISEVQKRKKE 1055
Cdd:PRK03918 492 ESELIKLKELAEQLKELEEKLKKynleelekKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
202-511 |
7.23e-06 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 50.24 E-value: 7.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 202 KAKKELSQAREYIEKIDIRINEVRANLEKLK-KEKEDAEKYTVYNKKLKVTKYILTSKKVEF------------------ 262
Cdd:pfam06160 83 KAKKALDEIEELLDDIEEDIKQILEELDELLeSEEKNREEVEELKDKYRELRKTLLANRFSYgpaidelekqlaeieeef 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 263 --------------LKMVLDETKDEIEALKEtkncYIQDISNIDSEiigLKVKINELVNELNEkGSEEVMELHKSIKELE 328
Cdd:pfam06160 163 sqfeeltesgdyleAREVLEKLEEETDALEE----LMEDIPPLYEE---LKTELPDQLEELKE-GYREMEEEGYALEHLN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 329 V--NLNNDKNALENAIDDLKhTLKMEESKNNdLNETKEKINNIrIDTLKKEAEAKvliKEIEKlneERQNLEKKVEQSES 406
Cdd:pfam06160 235 VdkEIQQLEEQLEENLALLE-NLELDEAEEA-LEEIEERIDQL-YDLLEKEVDAK---KYVEK---NLPEIEDYLEHAEE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 407 QVKALKN--QESKLSERINDTQKELY-GLKNELNQLENtlnnrtfdyqKNNETIENLTNQIAEFSDLEDT-KKLYKELED 482
Cdd:pfam06160 306 QNKELKEelERVQQSYTLNENELERVrGLEKQLEELEK----------RYDEIVERLEEKEVAYSELQEElEEILEQLEE 375
|
330 340
....*....|....*....|....*....
gi 33578097 483 IAVELEFSKKKLQEKITERNDSQSKLDNL 511
Cdd:pfam06160 376 IEEEQEEFKESLQSLRKDELEAREKLDEF 404
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
190-443 |
8.17e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 8.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 190 VSGVAEFDEKSEKAKKELSQAREYIEKIDIRIN------EVRANLEKLKKEKEDAEKytvynkklkvtkyiltskKVEFL 263
Cdd:PRK02224 467 VETIEEDRERVEELEAELEDLEEEVEEVEERLEraedlvEAEDRIERLEERREDLEE------------------LIAER 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 264 KMVLDETKDEIEALKETKncyiqdiSNIDSEIiglkvkinELVNELNEKGSEEVMELHKSIKELEVNLNNDKNALEnAID 343
Cdd:PRK02224 529 RETIEEKRERAEELRERA-------AELEAEA--------EEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE-SLE 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 344 DLKHTLKMEESKNNDLNETKEK------INNIRIDTL------KKEAEAKVLIKEIEKLNEERQNLEKKVEQSESQVKAL 411
Cdd:PRK02224 593 RIRTLLAAIADAEDEIERLREKrealaeLNDERRERLaekrerKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDEL 672
|
250 260 270
....*....|....*....|....*....|....*
gi 33578097 412 KNQESKLSERI---NDTQKELYGLKNELNQLENTL 443
Cdd:PRK02224 673 REERDDLQAEIgavENELEELEELRERREALENRV 707
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
116-518 |
8.38e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.12 E-value: 8.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 116 EVEKQNTKIN--TESSQKKTSKASKVEKRRRMKKNEVLDLLSKISliadgpniilqgdllriidTSPNERRKILDEVSGV 193
Cdd:pfam15921 445 QMERQMAAIQgkNESLEKVSSLTAQLESTKEMLRKVVEELTAKKM-------------------TLESSERTVSDLTASL 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 194 AEFDEKSEKAKKELSQAREyieKIDIRINEvranLEKLKKEKEDAEKYTVYNKKLKVtKYILTSKKVEFLKMVLDETKDE 273
Cdd:pfam15921 506 QEKERAIEATNAEITKLRS---RVDLKLQE----LQHLKNEGDHLRNVQTECEALKL-QMAEKDKVIEILRQQIENMTQL 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 274 IEALKETKNCYIQDISNIDSEIIGLKVKINELvNELNEKGSEEVMELHKSIKELE---VNLNNDKNALENAIDDLKHTLK 350
Cdd:pfam15921 578 VGQHGRTAGAMQVEKAQLEKEINDRRLELQEF-KILKDKKDAKIRELEARVSDLElekVKLVNAGSERLRAVKDIKQERD 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 351 --MEESKN--NDLNETKE-----------KINNIRIDTLKKEAEAKVLIKEIEKLNEERQNLE--------------KKV 401
Cdd:pfam15921 657 qlLNEVKTsrNELNSLSEdyevlkrnfrnKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgsdghamkvamgmqKQI 736
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 402 EQSESQVKALKNQESKLSERINDTQKELYGLKNELNQLENTLNNRTFDYQKNNETIENLTNQiaefsdledTKKLYKELE 481
Cdd:pfam15921 737 TAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQ---------ERRLKEKVA 807
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 33578097 482 DIAVELEfsKKKLQ----EKITERNDSQS-KLDNLHSEYVKE 518
Cdd:pfam15921 808 NMEVALD--KASLQfaecQDIIQRQEQESvRLKLQHTLDVKE 847
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
698-1178 |
8.49e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 8.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 698 KKLTNLSEDIKELEQILSNVKD--EIERLNNKINTCSTRKLELDNRLK----IARDQEFKKEEITKSNNLKIKELNMLNS 771
Cdd:COG4717 109 AELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELEERLEelreLEEELEELEAELAELQEELEELLEQLSL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 772 KIDDEISELTDEKEILSQKVQNLDNKLSEVMGQRERIVNEIKSYENSELSKRIKEidhKIRENE---------------- 835
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE---RLKEARlllliaaallallglg 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 836 SSKNTLENEIKKGAILV--------------KEVLIPKISELNSNIKSLADKKNMFKNSVEIYKSNIESNSSILSDKRGK 901
Cdd:COG4717 266 GSLLSLILTIAGVLFLVlgllallflllareKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 902 YEELTKGLKDLTDKKE-----CYELEIENLQN-----NKEELREKATDIDNQVNvINVDRAKYETRLEEEERKLYLCDTL 971
Cdd:COG4717 346 IEELQELLREAEELEEelqleELEQEIAALLAeagveDEEELRAALEQAEEYQE-LKEELEELEEQLEELLGELEELLEA 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 972 ENIEDISDEMIE-----ETYSLEIDDLERNQALLESSIKKLEpvnmrAIEDYDFINERYEELFGKRKEYEqEEGKYLQLI 1046
Cdd:COG4717 425 LDEEELEEELEEleeelEELEEELEELREELAELEAELEQLE-----EDGELAELLQELEELKAELRELA-EEWAALKLA 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1047 SEVQKRKKETFMKTY-DRVAENYEQIYGEI-GGNGKLSLENEEDPFSggllidASPMNKQLQNLDVMSGGEKSLTALAFL 1124
Cdd:COG4717 499 LELLEEAREEYREERlPPVLERASEYFSRLtDGRYRLIRIDEDLSLK------VDTEDGRTRPVEELSRGTREQLYLALR 572
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 33578097 1125 FAIQRL---NPSPFyVLDEVDAALDTKNASLIGDMISNASKESQFIVISHREQMISK 1178
Cdd:COG4717 573 LALAELlagEPLPL-ILDDAFVNFDDERLRAALELLAELAKGRQVIYFTCHEELVEL 628
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
205-441 |
8.50e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 8.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 205 KELSQAREYIEKidirineVRANLEKLKKEKEDAEKYTVYNKKLKVTKYILT-------SKKVEFLKMVLDETKDEIEAL 277
Cdd:COG4913 235 DDLERAHEALED-------AREQIELLEPIRELAERYAAARERLAELEYLRAalrlwfaQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 278 KEtkncyiqDISNIDSEIIGLKVKINELVNELNEKGSEEVMELHKSIKELEVnlnnDKNALENAIDDLKHTLKmeesknn 357
Cdd:COG4913 308 EA-------ELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLER----ELEERERRRARLEALLA------- 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 358 dlnetkekinniridTLKKEAEAkvlikEIEKLNEERQNLEKKVEQSESQVKALKNQESKLSERINDTQKELYGLKNELN 437
Cdd:COG4913 370 ---------------ALGLPLPA-----SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
....
gi 33578097 438 QLEN 441
Cdd:COG4913 430 SLER 433
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
4-86 |
8.74e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.99 E-value: 8.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSF-KNTKLKIPDGFTAILGPNGSGKSNTIDGICFVLGKTSAKSLRAGKFNQLITyhnGKRADYAEVTLFF 82
Cdd:cd03240 1 IDKLSIRNIRSFhERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGGAHDPKLI---REGEVRAQVKLAF 77
|
....
gi 33578097 83 DNIN 86
Cdd:cd03240 78 ENAN 81
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
214-525 |
8.76e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.21 E-value: 8.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 214 IEKIDIRInevrANLEKLKKEKEDAEKYTVYNKKLKVTKYILTSKKVEFLKMVLDETKDEIEALKetkncyiQDISNIDS 293
Cdd:pfam10174 235 IEMKDTKI----SSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLK-------QELSKKES 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 294 EIIGLKVKINELVNELNE-KGSEEVMELHKSIKELEVN-LNNDKNALENAIDDLKHTLKMEESKNNDLNETKE----KIN 367
Cdd:pfam10174 304 ELLALQTKLETLTNQNSDcKQHIEVLKESLTAKEQRAAiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKStlagEIR 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 368 NIRiDTLK-KEAEAKVLIKEIEKLNEERQNLEKKVEQSESQVKALKNQESKlseriNDTQkelyglkneLNQLENTLNNR 446
Cdd:pfam10174 384 DLK-DMLDvKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSN-----TDTA---------LTTLEEALSEK 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 447 tfdyqknNETIENLTNQIA--EFSDLEDTKKLYKELEDIAVELEFSKKKLQEKITERNDSQSKLDNLHSEYVKENARIKT 524
Cdd:pfam10174 449 -------ERIIERLKEQREreDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKS 521
|
.
gi 33578097 525 L 525
Cdd:pfam10174 522 L 522
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
4-332 |
8.94e-06 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 49.52 E-value: 8.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSFKNTKLKIPDGFTAILGPNGSGKSNTIDGICFVLGKTSAKSLRAGKFNQLITYHNGKRADYAEvtlfFD 83
Cdd:pfam13175 3 IKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEALDIFLNNKEKFFEDDFLVLYLKDVIKIDKEDLNI----FE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 84 NINREIPIDsdkvgICRKVKLNGDNnyyvvwYEVEKQNTKINTESSQKKTSKASKVEKRRRMKKNEVLDLLSKISLIADG 163
Cdd:pfam13175 79 NISFSIDIE-----IDVEFLLILFG------YLEIKKKYLCLASKGKAKEYEKTLHPKGANKADLLLELKISDLKKYLKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 164 PNIILQGDLLRIIDTSPNERRKILDEVSGVAEFDEKSEKA-KKELSQAREYIEKIDIRINEVRANLEKLKKEKE-DAEKY 241
Cdd:pfam13175 148 FKIYIYNNYYLDEKKNVFDKKSKYELPSLKEEFLNSEKEEiKVDKEDLKKLINELEKSINYHENVLENLQIKKLlISADR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 242 TVYNKKLKVTKYILTSKKVEFLKMVLDETKDEIEALKETKNcyiqDISNIDSEIIG-----LKVKINELVNELNEKGSEE 316
Cdd:pfam13175 228 NASDEDSEKINSLLGALKQRIFEEALQEELELTEKLKETQN----KLKEIDKTLAEelkniLFKKIDKLKDFGYPPFLNP 303
|
330
....*....|....*.
gi 33578097 317 VMELHKSIKELEVNLN 332
Cdd:pfam13175 304 EIEIKKDDEDLPLNKN 319
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
315-549 |
1.04e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 315 EEVMELHKSIKELEVNLNNDKNALENAIDDLKhtlkmeeSKNNDLNETKEKINNIRIDTLKKEAEAKVLIKEIEKLNEER 394
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLA-------ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 395 QNLEKKVEQ---------SESQVKALKNQES------------KLSERINDTQKELYGLKNELNQLENTLNnrtfdyQKN 453
Cdd:COG4942 100 EAQKEELAEllralyrlgRQPPLALLLSPEDfldavrrlqylkYLAPARREQAEELRADLAELAALRAELE------AER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 454 NETIENLTNQIAEFSDLEDTKklyKELEDIAVELEFSKKKLQEKITERNDSQSKLDNLHSEYVKENARIKTLKDMENFSl 533
Cdd:COG4942 174 AELEALLAELEEERAALEALK---AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA- 249
|
250
....*....|....*.
gi 33578097 534 drAVKGVLDAKLPGVV 549
Cdd:COG4942 250 --ALKGKLPWPVSGRV 263
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
696-932 |
1.19e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.63 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 696 DMKKLTNLSEDIKELEQILSNVKDEIERLNNKINTCSTRKLELDNRLKIARDQEFKKEEITKSNNLKIKELNMLNSKIDD 775
Cdd:TIGR04523 66 DEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 776 EISELTDEKEILSQKVQNLDNKLSEVMGQRERIVNEIksyenSELSKRIKEIDHKIRENESSKNTLENEIKKGAILVKEV 855
Cdd:TIGR04523 146 EIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK-----LNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 856 --LIPKISELNSNIKSLADKKNMFKNSVEIYKSNIESNSSI-------LSDKRGKYEELTKGLKDLTDKKECYELEIENL 926
Cdd:TIGR04523 221 seLKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEqnkikkqLSEKQKELEQNNKKIKELEKQLNQLKSEISDL 300
|
....*.
gi 33578097 927 QNNKEE 932
Cdd:TIGR04523 301 NNQKEQ 306
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
181-514 |
1.35e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 181 NERRKILDEVSGVAEFDEKSEKAKKELSQAREYIEKIDIRINEVRANLEKLKKEKEDA----EKYTVYNKKLKVTKYILT 256
Cdd:PRK02224 346 SLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDApvdlGNAEDFLEELREERDELR 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 257 SKKVEF---LKMVlDETKDEIEALKETKNCyiqdisnidsEIIGLKVKINELVNELNEKgSEEVMELHKSIKELEVnlnn 333
Cdd:PRK02224 426 EREAELeatLRTA-RERVEEAEALLEAGKC----------PECGQPVEGSPHVETIEED-RERVEELEAELEDLEE---- 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 334 DKNALENAIDDLKhTLKMEESKNNDLNETKEKINNiRIDTLKKEAEAKVLikEIEKLNEERQNLEKKVEQSESQVKALKN 413
Cdd:PRK02224 490 EVEEVEERLERAE-DLVEAEDRIERLEERREDLEE-LIAERRETIEEKRE--RAEELRERAAELEAEAEEKREAAAEAEE 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 414 QESKLSERINDTQKELYGLKNELNQLeNTLNNRTFDYQKNNETIENLTNQIAEFSDLEDTKK------------LYKELE 481
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALAELNDERRerlaekrerkreLEAEFD 644
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 33578097 482 DIAVELEFSKK------------KLQEKITERNDSQSKLDNLHSE 514
Cdd:PRK02224 645 EARIEEAREDKeraeeyleqveeKLDELREERDDLQAEIGAVENE 689
|
|
| YydB |
COG5293 |
Uncharacterized conserved protein YydD, contains DUF2326 domain [Function unknown]; |
198-468 |
1.41e-05 |
|
Uncharacterized conserved protein YydD, contains DUF2326 domain [Function unknown];
Pssm-ID: 444096 [Multi-domain] Cd Length: 572 Bit Score: 49.18 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 198 EKSEKAKKELSQAREY--IEKIDIRINEVRANLEKLKKE----KEDAEKYTVynkklkVTKYILTSKKVEFLKMVLDETK 271
Cdd:COG5293 190 KEEIKELKKLRKALKDelIGSVVKSISELRAEILELEEEieklEKDLEKFDV------AENYEELEKELDELKREINELR 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 272 DEIEALKETKNCYIQDISN---ID-SEIIGLKVKINELVNELNEKGSEEVMELHKSIkelevnLNNDKNALENAIDDLKH 347
Cdd:COG5293 264 NERYSLERRLKKIERSLEEeidIDpDELEKLYEEAGVFFPDQVKKRFEEVEAFHKSI------VENRREYLEEEIAELEA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 348 TLKmeesknnDLNETKEKINNIRIDTLK--KEAEA----KVLIKEIEKLNEERQNLEKKVEQSESQVKALKNQESKLSER 421
Cdd:COG5293 338 ELE-------ELEAELAELGKERAELLSllDSKGAldkyKELQEELAELEAELEELESRLEKLQELEDEIRELKEERAEL 410
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 33578097 422 INDTQKELYGLKNELNQLENT---LNNRTFDYQKNNETIENLTNQIAEFS 468
Cdd:COG5293 411 KEEIESDIEERKELLDEINKLfseIVEELYGNRKASLSIEVNKQGHLDFD 460
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
692-1066 |
1.98e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 692 KVDIDMKKLTNLSEDIKELEQILSNVKDEIERLNNKINTCSTRKLELDNRLKIARDQEFKKEEITKSNNLKIKeLNMLNS 771
Cdd:PRK03918 225 KLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-LSEFYE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 772 KIDDEISELTDEKEILSQKVQNLDNKLSEVMGQRERIvNEIKSyENSELSKRIKEIDHKIRENESSKNTLENEIKkgaiL 851
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL-EELKK-KLKELEKRLEELEERHELYEEAKAKKEELER----L 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 852 VKEVLIPKISELNSNIKSLADKKNMFKNSVEIYKSNIESNSSILSDKRGKYEELTKGL-------KDLTDK-----KECY 919
Cdd:PRK03918 378 KKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgRELTEEhrkelLEEY 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 920 ELEIENLQNNKEELREKATDIDNQVnvinvdrAKYETRLEEEERKLYLCDTLENIEDISdemiEETYSLEIDDLERNQAL 999
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKEL-------RELEKVLKKESELIKLKELAEQLKELE----EKLKKYNLEELEKKAEE 526
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33578097 1000 LESSIKKLEPVNMRAIEDYDFInERYEELFGKRKEYEQEEGKYLQLISEVQKRKKETFMKTYDRVAE 1066
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKEL-EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEE 592
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
150-407 |
2.23e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 150 VLDLLSKISLIADGPNIILQgdlLRIIDTSPNERRKILDEVsgVAEFDEKSEKAKK-ELSQAREYIEKidiRINEVRANL 228
Cdd:COG3206 120 IERLRKNLTVEPVKGSNVIE---ISYTSPDPELAAAVANAL--AEAYLEQNLELRReEARKALEFLEE---QLPELRKEL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 229 EKLKKEKED-AEKYTVYN----KKLKVTKYILTSKKVEFLKMVLDETKDEIEALKETKNCYIQDISNI--DSEIIGLKVK 301
Cdd:COG3206 192 EEAEAALEEfRQKNGLVDlseeAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELlqSPVIQQLRAQ 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 302 INELVNELNE------KGSEEVMELHKSIKELEVNLnndKNALENAIDDLKHTLKMEESKNNDLNETKEKINNIRIDTLK 375
Cdd:COG3206 272 LAELEAELAElsarytPNHPDVIALRAQIAALRAQL---QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE 348
|
250 260 270
....*....|....*....|....*....|..
gi 33578097 376 KEAEAKVLIKEIEKLNEERQNLEKKVEQSESQ 407
Cdd:COG3206 349 LEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
692-1056 |
2.45e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 692 KVDIDMKKLTNLSEDIKELEQILSNVKDEIERLNNKINTCSTRKLELDNRLKIARDQEFKKEEITKSNNLKIKELNMLNS 771
Cdd:TIGR04523 139 NIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLES 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 772 KIDD---EISELTDEKEILSQKVQNLDNKLSEVMGQRERIVNEiKSYENSELSKRIKEIDH---KIRENESSKNTLENEI 845
Cdd:TIGR04523 219 QISElkkQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE-QNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEI 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 846 -----KKGAILVKEV------LIPKISELNSNIKSLADKKNMFKNSVEIYKSNIESNSSILSDKRGKYEELTKGLKDLTD 914
Cdd:TIGR04523 298 sdlnnQKEQDWNKELkselknQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKK 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 915 KKECYELEIENLQNNKEELREKATDID--NQVNVINVDRAKYETRLEEEERKLYLCDTLENIEDISDeMIEETYSLE--I 990
Cdd:TIGR04523 378 ENQSYKQEIKNLESQINDLESKIQNQEklNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD-LTNQDSVKEliI 456
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33578097 991 DDLERNQALLESSIKKLEpvnmraiedyDFINERYEELFGKRKEYEQEEGKYLQLISEVQKRKKET 1056
Cdd:TIGR04523 457 KNLDNTRESLETQLKVLS----------RSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
334-523 |
2.69e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 334 DKNALENAIDDLKHTLKMEESKNNDLNETKEkinniRIDTLKKEAEAkvLIKEIEKLNEERQNLEKKVEQSESQVKALKN 413
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSDDLAALEE-----QLEELEAELEE--LEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 414 QESKLSERINDT-------------------------QKELYGLKNELNQLENTLNNRTFDYqkNNETIENLTNQIAEFS 468
Cdd:COG4913 735 RLEAAEDLARLElralleerfaaalgdaverelrenlEERIDALRARLNRAEEELERAMRAF--NREWPAETADLDADLE 812
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 33578097 469 DLEDTKKLYKELEDIAVElEFsKKKLQEKITERndSQSKLDNLHSEYVKENARIK 523
Cdd:COG4913 813 SLPEYLALLDRLEEDGLP-EY-EERFKELLNEN--SIEFVADLLSKLRRAIREIK 863
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
314-526 |
3.21e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 314 SEEVMElhKSIKELEV--NLNNDKNALENAIDDLKHTLKMEESKNNDL----------NETKEKINNIrIDTLKK---EA 378
Cdd:COG3206 92 SRPVLE--RVVDKLNLdeDPLGEEASREAAIERLRKNLTVEPVKGSNVieisytspdpELAAAVANAL-AEAYLEqnlEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 379 EAKVLIKEIEKLNEERQNLEKKVEQSESQVKALKNQE----------------SKLSERINDTQKELYGLKNELNQLENT 442
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglvdlseeaklllqqlSELESQLAEARAELAEAEARLAALRAQ 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 443 L--NNRTFDYQKNNETIENLTNQIAEF-SDLEDTKKLYKELEDIAVELEFSKKKLQEKITERndSQSKLDNLHSEYVKEN 519
Cdd:COG3206 249 LgsGPDALPELLQSPVIQQLRAQLAELeAELAELSARYTPNHPDVIALRAQIAALRAQLQQE--AQRILASLEAELEALQ 326
|
....*..
gi 33578097 520 ARIKTLK 526
Cdd:COG3206 327 AREASLQ 333
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
771-965 |
4.16e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 771 SKIDDEISELTDEKEILSQKVQNLDNKLSEVMGQRERIVNEIKsyensELSKRIKEIDHKIRENESSKNTLENEIKK--- 847
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE-----ALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 848 ------GAILVKEVLipkiseLNSniKSLADkknmFKNSVEIYKSNIESNSSILsdkrgkyEELTKGLKDLTDKKECYEL 921
Cdd:COG3883 94 alyrsgGSVSYLDVL------LGS--ESFSD----FLDRLSALSKIADADADLL-------EELKADKAELEAKKAELEA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 33578097 922 EIENLQNNKEELREKATDIDNQVNvinvDRAKYETRLEEEERKL 965
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQA----EQEALLAQLSAEEAAA 194
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
314-487 |
4.36e-05 |
|
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).
Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 46.25 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 314 SEEVMELHKSIKELEVNLNNDKNALENAIDDLKHTLKMEESKNndLNETKEKINNIRIDTLKKEAEAKVLIKEIE----K 389
Cdd:cd21116 50 LNEIKPKLLSLPNDIIGYNNTFQSYYPDLIELADNLIKGDQGA--KQQLLQGLEALQSQVTKKQTSVTSFINELTtfknD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 390 LNEERQNLEKKVEQSESQV---KALKNQESKLSERINDTQKELYGLKNELNQLENTLNNrtfdYQKNNETIENLTNQIAE 466
Cdd:cd21116 128 LDDDSRNLQTDATKAQAQVavlNALKNQLNSLAEQIDAAIDALEKLSNDWQTLDSDIKE----LITDLEDAESSIDAAFL 203
|
170 180
....*....|....*....|.
gi 33578097 467 FSDLEDTKKLYKELEDIAVEL 487
Cdd:cd21116 204 QADLKAAKADWNQLYEQAKSL 224
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
704-937 |
6.39e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 6.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 704 SEDIKELEQILSNVKDEIERLNNKINTCSTRKLELDNRLKIARDQefkkeeITKSNNlKIKELNMLNSKIDDEISELTDE 783
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR------IAALAR-RIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 784 KEILSQKVQNLDNKLSEV------MGQRERIVNEIKSYENSELSKRIKEIDHKIRENESSKNTLENEIKKgailvkevLI 857
Cdd:COG4942 92 IAELRAELEAQKEELAELlralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE--------LA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 858 PKISELNSNIKSLADKKNMFKNSVEIYKSNIESNSSILSDKRGKYEELTKGLKDLTDKKECYELEIENLQNNKEELREKA 937
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
182-527 |
7.60e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 7.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 182 ERRKILDEVSGVAEFDEKSEKAKKELSQAREyIEKIDIRINEVRaNLEKLKKEKEDAEKYTVYNKKLK-VTKYILTSKKV 260
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADEAKKKAEEAKK-AEEAKKKAEEAK-KADEAKKKAEEAKKADEAKKKAEeAKKKADEAKKA 1505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 261 EFLKMVLDETKDEIEALKETKNCYIQDISNIDSEIIGLKVKINELVNELNE-KGSEEVMELHKSIKELEVNLNNDKNA-- 337
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElKKAEEKKKAEEAKKAEEDKNMALRKAee 1585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 338 ---LENAIDDLKHTLKMEESKNNDLNETKEKINNIRIDTLKKEAEAKVLIKEIEKLNEERQNLEKKVEQSESQVKALKNQ 414
Cdd:PTZ00121 1586 akkAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 415 ESKLSERINDTQKELYGLKNELNQLENTLNNRTFDYQKNNETIENLTNQIAEFSDLEDTKKLYKELEDIAVELEFSKKKL 494
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK 1745
|
330 340 350
....*....|....*....|....*....|...
gi 33578097 495 QEKITERNDSQSKLDNLHSEYVKENARIKTLKD 527
Cdd:PTZ00121 1746 AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-52 |
9.36e-05 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 44.16 E-value: 9.36e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 33578097 10 KNFKSFKNTKLKIPDG-FTAILGPNGSGKSNTIDGICFVLGKTS 52
Cdd:cd00267 10 GGRTALDNVSLTLKAGeIVALVGPNGSGKSTLLRAIAGLLKPTS 53
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
181-955 |
1.00e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.97 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 181 NERRKILDEVSGVAEFDEKSEKAKKELSQA-REYIEKID--IRINEVRANLEKLKKEKEDAEKYTvynKKLKVTKYILTS 257
Cdd:TIGR01612 555 NWKKLIHEIKKELEEENEDSIHLEKEIKDLfDKYLEIDDeiIYINKLKLELKEKIKNISDKNEYI---KKAIDLKKIIEN 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 258 KKVEFLKMVLDETKDEIEALKETKNCYiqdiSNIDSEIIGL-KVKINELVNELNEkgseevmelhkSIKELEVNLNNDKN 336
Cdd:TIGR01612 632 NNAYIDELAKISPYQVPEHLKNKDKIY----STIKSELSKIyEDDIDALYNELSS-----------IVKENAIDNTEDKA 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 337 ALenaiDDLKHTLKMEESKNNDLNETKEKINNIRIDTLKKEAEAKVLIKEIEKLNEERQNLEKKVEQSESQVKALK---N 413
Cdd:TIGR01612 697 KL----DDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHIHGEINKDLNKILEDFKNKEKELSnkiN 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 414 QESKLSERINDTQKELYGLKNELNQLENTLNNRTFDYQKNNETIENLTNQIAEFSDleDTKKLYKELEDIAVELefsKKK 493
Cdd:TIGR01612 773 DYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKED--EIFKIINEMKFMKDDF---LNK 847
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 494 LQEKITERNDSQSKLDNLHSEYVKENARIKTlkDMENFSLDRAVKGVLDAKlPGVVDIAGNLAKTKGEYKTAIEVAGGAR 573
Cdd:TIGR01612 848 VDKFINFENNCKEKIDSEHEQFAELTNKIKA--EISDDKLNDYEKKFNDSK-SLINEINKSIEEEYQNINTLKKVDEYIK 924
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 574 LNHIVVKKMDDGSRAINYLKQKRLGRATFLPMDRIKGMDAKDISDTGIIGKAIDLVEfdikytnvfkfIFGNTHIVDNLE 653
Cdd:TIGR01612 925 ICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLIDKINELDK-----------AFKDASLNDYEA 993
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 654 NAKKLsLKYkarFVTLEGEVIEPSGAMVGGNIRRNSAIKVDIDmKKLTNLSEDIKELEQILS----NVKDEIERLNNK-- 727
Cdd:TIGR01612 994 KNNEL-IKY---FNDLKANLGKNKENMLYHQFDEKEKATNDIE-QKIEDANKNIPNIEIAIHtsiyNIIDEIEKEIGKni 1068
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 728 ----------INTCSTRKLELDNRLKIARDQEFKKEEitksnnlkikelnmlNSKIDDEISELTDEKEILSQKVQNLDNK 797
Cdd:TIGR01612 1069 ellnkeileeAEINITNFNEIKEKLKHYNFDDFGKEE---------------NIKYADEINKIKDDIKNLDQKIDHHIKA 1133
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 798 LSEVMGQRERIVNEIKSYENSELSKRIKEI-DHKIRENESSKNTLENEIKKGAILVKEV--LIPKISELNSNIKSLADKK 874
Cdd:TIGR01612 1134 LEEIKKKSENYIDEIKAQINDLEDVADKAIsNDDPEEIEKKIENIVTKIDKKKNIYDEIkkLLNEIAEIEKDKTSLEEVK 1213
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 875 NMfknsveiyksNIESNSSILSDKRGKYEELTKGLKDLTDKKECYELEIENLQNNKEELREK---ATDIDNQVNVINVDR 951
Cdd:TIGR01612 1214 GI----------NLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEmgiEMDIKAEMETFNISH 1283
|
....
gi 33578097 952 AKYE 955
Cdd:TIGR01612 1284 DDDK 1287
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
359-524 |
1.06e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 359 LNETKEKINNIRIDTLKKEAEAKVLIKEIEKLNEERQNLEKKVEQSESQVKALKNQESKLSERIND--TQKELYGLKNEL 436
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrNNKEYEALQKEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 437 NQLEntlnnrtfdyqknnETIENLTNQIAEFSDLEDTKKlyKELEDIAVELEFSKKKLQEKITERNDSQSKLDNLHSEYV 516
Cdd:COG1579 99 ESLK--------------RRISDLEDEILELMERIEELE--EELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
....*...
gi 33578097 517 KENARIKT 524
Cdd:COG1579 163 AEREELAA 170
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
240-1070 |
1.44e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 240 KYTVYNKKLKVTKYILTSKKVEFLKMVLDETKDEIEALKETKNCYIQDISNIDSEIIGLKVKINELvnelnEKGSEEVME 319
Cdd:TIGR00606 192 RQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEI-----EHNLSKIMK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 320 LHKSIKELevnlnnDKNALENAIDDLKHTLKMEESKNNDLNETKEKINNIRIDTLKKEAEAKVLIKEIEKLNEERQNLEK 399
Cdd:TIGR00606 267 LDNEIKAL------KSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQ 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 400 K-----VEQSESQVKALKNQESKL---SERI-NDTQKELYGLKNELNQLENTLNNRTFDYQKNNETIENLTNQIAEFSDL 470
Cdd:TIGR00606 341 EktellVEQGRLQLQADRHQEHIRardSLIQsLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSK 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 471 EDTKKlyKELEDIAVELEFSKKKLQEKITERNDSQSKLDNLHSEYVKENARIKTLkdmenFSLDRAVKGVLdAKLPGVVD 550
Cdd:TIGR00606 421 ERLKQ--EQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRI-----LELDQELRKAE-RELSKAEK 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 551 IAGNLAKTKGEYKTAIEVAGGARLNHIVVKKMDDGSRAINYLKQ-KRLGRATFLPMDRIKgmDAKDISDTGIIGKAIDlv 629
Cdd:TIGR00606 493 NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQmEMLTKDKMDKDEQIR--KIKSRHSDELTSLLGY-- 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 630 efdikytnvfkfiFGNTHIV-DNLENAKKLSLKYKARFVTLEGEViePSGAMVGGNIRRNSAIKVDIDMKKLTNLSE--D 706
Cdd:TIGR00606 569 -------------FPNKKQLeDWLHSKSKEINQTRDRLAKLNKEL--ASLEQNKNHINNELESKEEQLSSYEDKLFDvcG 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 707 IKELEQILSNVKDEIERLNNKINTCSTRKLELDNRLKIARDQEFKKEEITKSNNLKIKELNMLNSKIDDEISELTDEKEI 786
Cdd:TIGR00606 634 SQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKS 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 787 LSQKVQNLDNKLSEVMGQRE-------RIVNEIKSYENS--ELSKRIKEIDHKIRENESSKNTLENEIKKGAILVKEV-L 856
Cdd:TIGR00606 714 TESELKKKEKRRDEMLGLAPgrqsiidLKEKEIPELRNKlqKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVtI 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 857 IPKISELNSNIKSLADKKNMFKNSVEIYKSNIESNSSIlSDKRGKYEELTKGLKDLTDKKECYELEIENLQNNKEELREK 936
Cdd:TIGR00606 794 MERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEK-QEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 937 ATDIDNQVNvinvDRAKYETRLEEEERKLYLCDTleNIEDISDEMIEETYSLEiDDLERNQALlessIKKLEPVNMRAIE 1016
Cdd:TIGR00606 873 KLQIGTNLQ----RRQQFEEQLVELSTEVQSLIR--EIKDAKEQDSPLETFLE-KDQQEKEEL----ISSKETSNKKAQD 941
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 33578097 1017 DYDFINERYEELFGKRKEYEqeegKYLQLISEVQKRKKETFMKTYDRVAENYEQ 1070
Cdd:TIGR00606 942 KVNDIKEKVKNIHGYMKDIE----NKIQDGKDDYLKQKETELNTVNAQLEECEK 991
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
698-949 |
1.46e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 698 KKLTNLSEDIKELEQILSNVKDEIERLNNKINTCSTRKLELDNRLKIardqefkkeeitksNNLKIKELNMLNSKIDDEI 777
Cdd:TIGR04523 47 NELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKK--------------NKDKINKLNSDLSKINSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 778 SELTDEKEILSQKVQNLDNKLSEVMGQRERIVNEIKSYEN--SELSKRIKEIDHKIRENESSKNTLENEIK--------- 846
Cdd:TIGR04523 113 KNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKelEKLNNKYNDLKKQKEELENELNLLEKEKLniqknidki 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 847 KGAILVKEVLIPKISELNSNIKSLADKKNMFKNSVEIYKSNIESNSSILSDKRGKYEELTKGLKDLTDKKECYELEIENL 926
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
250 260
....*....|....*....|...
gi 33578097 927 QNNKEELREKATDIDNQVNVINV 949
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKS 295
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-38 |
1.57e-04 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 45.52 E-value: 1.57e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 33578097 2 ISISEIHlKNFKSFK---NTKLKIPDG-FTAILGPNGSGKS 38
Cdd:COG1118 3 IEVRNIS-KRFGSFTlldDVSLEIASGeLVALLGPSGSGKT 42
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1112-1190 |
1.72e-04 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 45.52 E-value: 1.72e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33578097 1112 SGGEKSLTALAFLFaiqrLNPSPFYVLDEVDAALDTKNASLIGDMISNASKESQFIVISHREQMISKSNVMygVCMENG 1190
Cdd:COG4988 475 SGGQAQRLALARAL----LRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRI--LVLDDG 547
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
703-958 |
1.96e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.66 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 703 LSEDIKELEQILSNVKDEIERLNNKINTCSTRKLELDNRLKIARDQEFKKEEITKSNNLKIKELNMLNSKIdDEISELTD 782
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSAL-NELSSLED 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 783 EKEILSQKVQNLDNKLSEVmgqrERIVNEIKSYEnSELSKRIKEIDHKIRENESSKNTLENEIKKGAILVKEvLIPKISE 862
Cdd:PRK01156 250 MKNRYESEIKTAESDLSME----LEKNNYYKELE-ERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSN-IDAEINK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 863 LNSNIKSLADKKNmFKNSVEIYKSNIESNSSILSDKRG---KYEELTKGLKDLTDKKECYELEIENLQNNKEELREKA-- 937
Cdd:PRK01156 324 YHAIIKKLSVLQK-DYNDYIKKKSRYDDLNNQILELEGyemDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQei 402
|
250 260
....*....|....*....|...
gi 33578097 938 --TDIDNQVNVINVDRAKYETRL 958
Cdd:PRK01156 403 dpDAIKKELNEINVKLQDISSKV 425
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
101-510 |
1.97e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 45.98 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 101 KVKLNGDNNYYVVWYEVEKQNTKINTESSQKKTSKASKVEkrrrmkknevldLLSKISLIADGPNIILQGD-LLRIIDTS 179
Cdd:PTZ00440 443 EIKKKYDEKINELKKSINQLKTLISIMKSFYDLIISEKDS------------MDSKEKKESSDSNYQEKVDeLLQIINSI 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 180 PNERRKILDEVSGVAEFDEKSEKAKKELSQAREYIEKIDIRINEVRANLEKLKKEKEDAEkytvynkklkvtkyiltsKK 259
Cdd:PTZ00440 511 KEKNNIVNNNFKNIEDYYITIEGLKNEIEGLIELIKYYLQSIETLIKDEKLKRSMKNDIK------------------NK 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 260 VEFLKMVLDETKDEIEALKETKNcYIQDISNIDSEIIGLKVKINELVNELNEKGSEEVMELHK-SIKELEVNLNNDKNAL 338
Cdd:PTZ00440 573 IKYIEENVDHIKDIISLNDEIDN-IIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKFYKgDLQELLDELSHFLDDH 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 339 EN------AIDDLKHTLKMEESKNNDLNETKEKINNIRIDTLKKEAEAKVLIKEI---EKLNEERQNLEKKVEQSESQVK 409
Cdd:PTZ00440 652 KYlyheakSKEDLQTLLNTSKNEYEKLEFMKSDNIDNIIKNLKKELQNLLSLKENiikKQLNNIEQDISNSLNQYTIKYN 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 410 ALKNqesklseRINDTQKELYGLKNELNQLENTLNNRTFDYQKNNETI---ENLTNQIAEFSDLEDTKKlyKELEDIAVE 486
Cdd:PTZ00440 732 DLKS-------SIEEYKEEEEKLEVYKHQIINRKNEFILHLYENDKDLpdgKNTYEEFLQYKDTILNKE--NKISNDINI 802
|
410 420
....*....|....*....|....
gi 33578097 487 LEFSKKKLQEKITERNDSQSKLDN 510
Cdd:PTZ00440 803 LKENKKNNQDLLNSYNILIQKLEA 826
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
9-94 |
2.02e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 44.18 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 9 LKNFKSFKN------TKLKiPDGFTAILGPNGSGKSNTIDGICFVL-GKTSakslRAGKFNQLITYHNgKRADYAEVTLF 81
Cdd:cd03279 8 LKNFGPFREeqvidfTGLD-NNGLFLICGPTGAGKSTILDAITYALyGKTP----RYGRQENLRSVFA-PGEDTAEVSFT 81
|
90
....*....|....*....
gi 33578097 82 FDN------INREIPIDSD 94
Cdd:cd03279 82 FQLggkkyrVERSRGLDYD 100
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
191-440 |
2.91e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 191 SGVAEFDEKSEKAKKELSQAREYIEKIDIRINEVRANLEKLKKEKEDaekytvYNKKLKVTKyiltsKKVEFLKMVLDET 270
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDE------LNAQVKELR-----EEAQELREKRDEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 271 KDEIEALKETKNCYIQDISNIDSEIIGLKVKINELvnelnEKGSEEVMELHKSIKELEVNLNN------DKNALENAIDD 344
Cdd:COG1340 70 NEKVKELKEERDELNEKLNELREELDELRKELAEL-----NKAGGSIDKLRKEIERLEWRQQTevlspeEEKELVEKIKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 345 LK---HTLKMEESKNNDLNETKEKINNIR---------IDTLKKEAEAKV-----LIKEIEKLNEERQNLEKKVEQSESQ 407
Cdd:COG1340 145 LEkelEKAKKALEKNEKLKELRAELKELRkeaeeihkkIKELAEEAQELHeemieLYKEADELRKEADELHKEIVEAQEK 224
|
250 260 270
....*....|....*....|....*....|...
gi 33578097 408 VKALKNQESKLSERINDTQKELYGLKNELNQLE 440
Cdd:COG1340 225 ADELHEEIIELQKELRELRKELKKLRKKQRALK 257
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
294-543 |
2.99e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.92 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 294 EIIGLKVKINELVNELNEKGSEEVMELHKSIKELEV-NLNNDKNALENAIDDLKHTLKMEESKNNDLNETKEK-----IN 367
Cdd:PRK05771 10 LIVTLKSYKDEVLEALHELGVVHIEDLKEELSNERLrKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKsleelIK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 368 NIRIDTLKKEAEAKVLIKEIEKLNEERQNLEKKVEqsesQVKALKNQESKLSerindtqkELYGLKNeLNQLENTLNNRT 447
Cdd:PRK05771 90 DVEEELEKIEKEIKELEEEISELENEIKELEQEIE----RLEPWGNFDLDLS--------LLLGFKY-VSVFVGTVPEDK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 448 FDYQKNNETIENLtnqiAEFSDLEDT--------KKLYKELEDIAVELEFSKKKLQEKIT---ERNDSQSKLDNLHSEYV 516
Cdd:PRK05771 157 LEELKLESDVENV----EYISTDKGYvyvvvvvlKELSDEVEEELKKLGFERLELEEEGTpseLIREIKEELEEIEKERE 232
|
250 260
....*....|....*....|....*..
gi 33578097 517 KENARIKTLKDmENFSLDRAVKGVLDA 543
Cdd:PRK05771 233 SLLEELKELAK-KYLEELLALYEYLEI 258
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
707-964 |
3.44e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.89 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 707 IKELEQILSnvkdEIERLNNKINTCSTRKLELDNRLKIAR----DQEFKKEEITKSNNLKIKELNMLNSKIDDEISELTD 782
Cdd:PLN02939 155 LEDLEKILT----EKEALQGKINILEMRLSETDARIKLAAqekiHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 783 EKE---ILSQKVQNLDNKLSEVMGQRERIVneiksyensELSKRIKEIDHKIRENESSKNTLENEIKKGAILVKEVLIPK 859
Cdd:PLN02939 231 LKEenmLLKDDIQFLKAELIEVAETEERVF---------KLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDCWWEK 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 860 IselnSNIKSLADKKnmfKNSVEIYKSNIESNssilSDKRGKYEELTKGLKDL-TDKKECYELEI--ENLQNNKEELREK 936
Cdd:PLN02939 302 V----ENLQDLLDRA---TNQVEKAALVLDQN----QDLRDKVDKLEASLKEAnVSKFSSYKVELlqQKLKLLEERLQAS 370
|
250 260 270
....*....|....*....|....*....|..
gi 33578097 937 ATDIDNQVNVINVDRAKYETRL----EEEERK 964
Cdd:PLN02939 371 DHEIHSYIQLYQESIKEFQDTLsklkEESKKR 402
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
703-940 |
3.56e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 703 LSEDIKELeQILSNV----KDEIERLNNKINTCSTRKLELDNRLKIARDQEFKKEEITKSNNL-----------KIKELN 767
Cdd:PHA02562 155 LVEDLLDI-SVLSEMdklnKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIArkqnkydelveEAKTIK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 768 MLNSKIDDEISELTDEKEILSQKVQNLDNKLSEVMGQRERIVNEIKSYENSEL----SKRIKEIDHKIRENESSKNTLEN 843
Cdd:PHA02562 234 AEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGVcptcTQQISEGPDRITKIKDKLKELQH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 844 EIKKgailvkevLIPKISELNsnikSLADKKNMFKNSVEIYKSNIESNSSILSDKRGKYEELTKGLKDLTDKKECYELEI 923
Cdd:PHA02562 314 SLEK--------LDTAIDELE----EIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEEL 381
|
250
....*....|....*..
gi 33578097 924 ENLQNNKEELREKATDI 940
Cdd:PHA02562 382 AKLQDELDKIVKTKSEL 398
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
195-1025 |
3.71e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 195 EFDEKSEKAKK-ELSQAREYIEKIDI--RINEVRANLEKLKKEK----EDAEKYTVYNKKLKVTKYiLTSKKVEFLKMVL 267
Cdd:PTZ00121 1155 EIARKAEDARKaEEARKAEDAKKAEAarKAEEVRKAEELRKAEDarkaEAARKAEEERKAEEARKA-EDAKKAEAVKKAE 1233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 268 DETKDEIEALKETKNCYIQDISNIDSEIIGLKVKINELVNELNEKGSEEVMELHKSIKELEVNLNNDKNALENAiddlkh 347
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEA------ 1307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 348 TLKMEESKNNDLNETKEKINNIRIDTLKKEAEAKVLIKEIEKLNEERQnlEKKVEQSESQVKALKNQESKLSERINDTQK 427
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAA--ADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 428 ELYGLK--NELNQLENTLNNRTFDYQKNNET---IENLTNQIAEFSDLEDTKKLYKElediAVELEFSKKKLQEKITERN 502
Cdd:PTZ00121 1386 KAEEKKkaDEAKKKAEEDKKKADELKKAAAAkkkADEAKKKAEEKKKADEAKKKAEE----AKKADEAKKKAEEAKKAEE 1461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 503 DSQSKLDNLHSEYVKENARIKTLKDMENFSLDRAVKGVLDAKLPGVVDIAGNLAKTKGEYKTAIEVAGGARlnhivVKKM 582
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE-----AKKA 1536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 583 DDGSRAINYLKQKRLGRATFL-PMDRIKGMDAKDISD---TGIIGKAIDLVEFDIKYTNVFKFIFGNTHIVDNLENAKKL 658
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELkKAEEKKKAEEAKKAEedkNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE 1616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 659 SLKYKARFVTLEGEV---IEPSGAMVGGNIRRNSAIKVDIDMKKLTNLSEDIKELE-----QILSNVKDEIERLNNKINT 730
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEkkkVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEdkkkaEEAKKAEEDEKKAAEALKK 1696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 731 CSTRKLELDNRLKIARDQEFKKEEITKS---NNLKIKELNML---NSKIDDEISELTDEKEILSQKVQNLDNKLSEVMGQ 804
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKKKAEELKKAeeeNKIKAEEAKKEaeeDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 805 RERIVNEIKSYENselSKRIKEIDHKIRENESSKNTLENEIKKGAILVKEVLIPKISElnsnIKSLADKKNMFKNSVEIY 884
Cdd:PTZ00121 1777 KEAVIEEELDEED---EKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSA----IKEVADSKNMQLEEADAF 1849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 885 KSNIESNSSILSDKRGKYEELTKGLKDLTDKKECYELEIENLQNNKEELREKATDI-----DNQVNVINVDRAKYETRLE 959
Cdd:PTZ00121 1850 EKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNnmagkNNDIIDDKLDKDEYIKRDA 1929
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33578097 960 EEERKLYLCDTLEN--IEDIS----DEMIEETYSLEIDDLERNQALLESSIKKLEPVNMRAIEDYDFINERY 1025
Cdd:PTZ00121 1930 EETREEIIKISKKDmcINDFSskfcDYMKDNISSGNCSDEERKELCCSISDFCLKYFDHNSNEYYDCMKEEF 2001
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
195-531 |
3.76e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.83 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 195 EFDEKSEKAKKELSQAREYIEKIDIRINEVRANLEKLKKEKEDAeKYTVYNKKLKVTKyiltskkvefLKMVLDETKDEI 274
Cdd:pfam12128 601 ELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFA-RTALKNARLDLRR----------LFDEKQSEKDKK 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 275 -EALKETKNCYIQDISNIDSEIIGLKVKINELVNELNEKGSEEVMELHKSIKELEVNLNNDKNALENAIDDLKHTLK--- 350
Cdd:pfam12128 670 nKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKael 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 351 --MEESKNNDLNetKEKINNIRIdtLKKEAEAKVLIKEIEKLNEERQnleKKVEQSESQVKALKNQESKLSERINDTQKE 428
Cdd:pfam12128 750 kaLETWYKRDLA--SLGVDPDVI--AKLKREIRTLERKIERIAVRRQ---EVLRYFDWYQETWLQRRPRLATQLSNIERA 822
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 429 LYGLKNELNQLENTLNNRTFDYQKNNETIENLTNQIAefsdlEDTKKLYKELEDIA-VELEFSKKKLQEKITERNDSQSK 507
Cdd:pfam12128 823 ISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLS-----ENLRGLRCEMSKLAtLKEDANSEQAQGSIGERLAQLED 897
|
330 340
....*....|....*....|....
gi 33578097 508 LDNLHsEYVKENARiktlKDMENF 531
Cdd:pfam12128 898 LKLKR-DYLSESVK----KYVEHF 916
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
205-510 |
4.48e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.65 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 205 KELSQAREYIEKIDIRINEVRANLEKLKKEKEdaekytVYNKKLKVTKYILTSKKVeflkmvldeTKDEIEALKETKNCY 284
Cdd:TIGR00606 744 KEIPELRNKLQKVNRDIQRLKNDIEEQETLLG------TIMPEEESAKVCLTDVTI---------MERFQMELKDVERKI 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 285 IQDISNIDSeiiglkVKINELVNELNEKGSEEVMELHKSIKELEVN--LNNDKNaleNAIDDLKHTLKMEESKNNDLNET 362
Cdd:TIGR00606 809 AQQAAKLQG------SDLDRTVQQVNQEKQEKQHELDTVVSKIELNrkLIQDQQ---EQIQHLKSKTNELKSEKLQIGTN 879
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 363 KEKINNIRIDTLKKEAEAKVLIKEIEKLNEERQNLE---KKVEQSESQVKALKNQESKLSE-RINDTQKELYGLKNELNQ 438
Cdd:TIGR00606 880 LQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLEtflEKDQQEKEELISSKETSNKKAQdKVNDIKEKVKNIHGYMKD 959
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33578097 439 LENTLNNRTFDYQKNNETieNLTNQIAEFSDLEDTKKLYKElEDIAVELEFSKKKLQEKITERNDSQSKLDN 510
Cdd:TIGR00606 960 IENKIQDGKDDYLKQKET--ELNTVNAQLEECEKHQEKINE-DMRLMRQDIDTQKIQERWLQDNLTLRKREN 1028
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
5-63 |
4.56e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 39.51 E-value: 4.56e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 5 SEIHLKNFKSFKNTKLKI-PDGFTAILGPNGSGKSNTIDGICFVLgkTSAKSLRagkFNQ 63
Cdd:pfam13555 2 TRLQLINWGTFDGHTIPIdPRGNTLLTGPSGSGKSTLLDAIQTLL--VPAKRAR---FNK 56
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
698-1057 |
5.60e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.66 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 698 KKLTNLSEDIKELEQILSNVKDEIERLNNKINTCSTRKLELDNRLKIARDqefKKEEITKSNNLKIKELNmlNSKIDDEI 777
Cdd:TIGR01612 565 KELEEENEDSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNISD---KNEYIKKAIDLKKIIEN--NNAYIDEL 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 778 SELTDEkeilsqkvqnldnKLSEVMGQRERIVNEIKsyenSELSKrIKEIDHKIRENESSKNTLENEIKKGAILVkevli 857
Cdd:TIGR01612 640 AKISPY-------------QVPEHLKNKDKIYSTIK----SELSK-IYEDDIDALYNELSSIVKENAIDNTEDKA----- 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 858 pKISELNSNIKSLADK-KNMFKNSVEIYKSNIESNSSILSD-----KRGKYEELTKGL----KDLTDKKECYELEIENLQ 927
Cdd:TIGR01612 697 -KLDDLKSKIDKEYDKiQNMETATVELHLSNIENKKNELLDiiveiKKHIHGEINKDLnkilEDFKNKEKELSNKINDYA 775
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 928 NNKEEL---REKATDIDNQVN-VINVDRAKYETRLEEEERKLYLCDTLENIEDISDEMIEETYSLEIDDLERNQALLESS 1003
Cdd:TIGR01612 776 KEKDELnkyKSKISEIKNHYNdQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFE 855
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 33578097 1004 IKKLEPVNMRAIEDYDFINERYEELFG-KRKEYEQEEGKYLQLISEVQKRKKETF 1057
Cdd:TIGR01612 856 NNCKEKIDSEHEQFAELTNKIKAEISDdKLNDYEKKFNDSKSLINEINKSIEEEY 910
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
269-527 |
5.96e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 269 ETKDEIEALKETKNCYIQDISNIDSEIIGLKVKINELVNELNEKGSEEVM---ELHKSIKELEVNLNNDKNALE--NAID 343
Cdd:TIGR00618 560 SLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMlacEQHALLRKLQPEQDLQDVRLHlqQCSQ 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 344 DLKHTLKMEESKNNDLNETKEKINNIRIDTLKKEAEAKVLIKEIEKLNEERQNLEKK--VEQSESQVKALKNQESKLSER 421
Cdd:TIGR00618 640 ELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKemLAQCQTLLRELETHIEEYDRE 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 422 INDTQKELYGLKNELNQLENTLNNRTFDYQKNNETIENLTNQIAEFSDLEDTKKLYK--ELEDIAVELEFSKKKLQEKIT 499
Cdd:TIGR00618 720 FNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTgaELSHLAAEIQFFNRLREEDTH 799
|
250 260
....*....|....*....|....*...
gi 33578097 500 ERNDSQSKldnlHSEYVKENARIKTLKD 527
Cdd:TIGR00618 800 LLKTLEAE----IGQEIPSDEDILNLQC 823
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
202-528 |
6.53e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 202 KAKKELSQAREYIEKIDIRINEVRANLEKLKKEKEDAEKYTVYNKKLKVTKYILTSKKVEFLKMVldETKDEIEALKETK 281
Cdd:PRK01156 302 KYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYN--SYLKSIESLKKKI 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 282 NCY---IQDISNIDSEIIGLKVKINELVNELNEKGSEEVMELHKSIKelevNLNNDKNALENAIDDLKHTLKMEESK--- 355
Cdd:PRK01156 380 EEYsknIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVS----SLNQRIRALRENLDELSRNMEMLNGQsvc 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 356 -------------------NNDLNETKEKINNIRIDTLKKEAEAKVLIKEIEKLN----EERQNLEKKVEQSESQVKALK 412
Cdd:PRK01156 456 pvcgttlgeeksnhiinhyNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLEseeiNKSINEYNKIESARADLEDIK 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 413 NQESKLSER---------------INDTQKELYGLKNELNQLEN----TLNNRTFDYQKNNETIENLTNQI-AEFSDLED 472
Cdd:PRK01156 536 IKINELKDKhdkyeeiknrykslkLEDLDSKRTSWLNALAVISLidieTNRSRSNEIKKQLNDLESRLQEIeIGFPDDKS 615
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 33578097 473 -TKKLYKELEDIAVELEFSKKKLQEKITERNDSQSKLDNLHSEYVKENARIKTLKDM 528
Cdd:PRK01156 616 yIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEI 672
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
182-523 |
6.86e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 182 ERRKILDEVSGVAEFDEKSEKAKKELSQAREYIEKIDIRINEVRANLEKLKKEKEDAEKYTVYNKKLKVTKYILTS---K 258
Cdd:PTZ00121 1299 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEeakK 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 259 KVEFLKMVLDETKDEIEALKET-----KNCYIQDISNIDSEIIGLKVKINEL--VNELNEKGSE--EVMELHKSIKELEV 329
Cdd:PTZ00121 1379 KADAAKKKAEEKKKADEAKKKAeedkkKADELKKAAAAKKKADEAKKKAEEKkkADEAKKKAEEakKADEAKKKAEEAKK 1458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 330 NLNNDKNALE-NAIDDLKHtlKMEESKNNDLNETKEKINNIRIDTLKKEAEAKVLIKEIEKLNEERQNLE-KKVEQSESQ 407
Cdd:PTZ00121 1459 AEEAKKKAEEaKKADEAKK--KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEaKKAEEAKKA 1536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 408 VKALKNQESKLSERINDTQK-ELYGLKNELNQLENTLNNRTFDYQKNNETIENLTNQIAEFSDLEDTKKLYKELEDIAVE 486
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEElKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE 1616
|
330 340 350
....*....|....*....|....*....|....*..
gi 33578097 487 LEFSKKKLQEKITERNDSQSKLDNLHSEYVKENARIK 523
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
697-847 |
8.38e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 697 MKKLTNLSEDIKELEQILSNVKDEIERLNNKINtcsTRKLELDNRLK---IARDQEFKKEEITKSNNL-----KIKELNM 768
Cdd:COG3883 50 NEEYNELQAELEALQAEIDKLQAEIAEAEAEIE---ERREELGERARalyRSGGSVSYLDVLLGSESFsdfldRLSALSK 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33578097 769 LNSKIDDEISELTDEKEILSQKVQNLDNKLSEVMGQRErivneiksyensELSKRIKEIDHKIRENESSKNTLENEIKK 847
Cdd:COG3883 127 IADADADLLEELKADKAELEAKKAELEAKLAELEALKA------------ELEAAKAELEAQQAEQEALLAQLSAEEAA 193
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
703-822 |
8.40e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.08 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 703 LSEDIKE-LEQILSNVKDEIERLNNKINTCSTRKL-----------ELDNRLKIARDQEFKKEEITKSNNLKIKELNMLN 770
Cdd:smart00787 141 LLEGLKEgLDENLEGLKEDYKLLMKELELLNSIKPklrdrkdaleeELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEI 220
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 33578097 771 SKIDDEISELTDEKEILSQKVQNLDNKLSEVMGQ---RERIVNEIKSYENSELSK 822
Cdd:smart00787 221 MIKVKKLEELEEELQELESKIEDLTNKKSELNTEiaeAEKKLEQCRGFTFKEIEK 275
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1112-1172 |
8.77e-04 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 43.61 E-value: 8.77e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33578097 1112 SGGEKSLTALA--FLfaiqrLNPsPFYVLDEVDAALDTKNASLIGDMISNASKESQFIVISHR 1172
Cdd:COG1132 478 SGGQRQRIAIAraLL-----KDP-PILILDEATSALDTETEALIQEALERLMKGRTTIVIAHR 534
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
307-466 |
1.01e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 307 NELNEKGSEEVMELHKSIKELEVNLNNDKNALENAIDDLKHTLKMEESKNNDLNETKEKINNIRIDTLKKEAEAKVLIKE 386
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 387 IEKLNEERQNLEKKVEQSESQVKALKNQESKLSERINDTQKELYGLKNELNQLENTLNNRTFDYQKNNETIENLTNQIAE 466
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
4-41 |
1.03e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 42.26 E-value: 1.03e-03
10 20 30
....*....|....*....|....*....|....*...
gi 33578097 4 ISEIHLKNFKSFKNTKLKIPDgFTAILGPNGSGKSNTI 41
Cdd:COG4938 1 IKSISIKNFGPFKEAELELKP-LTLLIGPNGSGKSTLI 37
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
214-534 |
1.13e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 43.50 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 214 IEKIDIRINEVRANLEKLKKEKEDAEKYTV----YNKKLKVTKYILTSKKVEFLKMVLDETKDEIEALKET--KNCYIQD 287
Cdd:PTZ00108 1054 KKSEKITAEEEEGAEEDDEADDEDDEEELGaavsYDYLLSMPIWSLTKEKVEKLNAELEKKEKELEKLKNTtpKDMWLED 1133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 288 ISNIDSEIIGLKvkiNELVNELNEkgseevmELHKSIKELEVNLNNDKNALENAIDDLKHTLKMEESKNNDLNETKEKIN 367
Cdd:PTZ00108 1134 LDKFEEALEEQE---EVEEKEIAK-------EQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDS 1203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 368 NIRIDTLKKEAEAKVLIKEIEKLNEERQNLEKKVEQSESQVKALKNQESKlSERINDTQKELYGLKNELNQLENTLNNRT 447
Cdd:PTZ00108 1204 DEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKS-SEDNDEFSSDDLSKEGKPKNAPKRVSAVQ 1282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 448 FDYQKNNETIENLTNQIAEFSDlEDTKKLYKELEDIAVELEFSKKKLQEKITERNDSQSKLDNLHSEYVKENARIKTLKD 527
Cdd:PTZ00108 1283 YSPPPPSKRPDGESNGGSKPSS-PTKKKVKKRLEGSLAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKS 1361
|
....*..
gi 33578097 528 MENFSLD 534
Cdd:PTZ00108 1362 DSSSEDD 1368
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
335-482 |
1.17e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 335 KNALENAIDDLKHTLK--MEESKNNDLNETKEKINNIRIDTLKKEAEAKvliKEIEKLNEERQNLEKKVEQSESQVKalk 412
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKriLEEAKKEAEAIKKEALLEAKEEIHKLRNEFE---KELRERRNELQKLEKRLLQKEENLD--- 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 413 nqesKLSERINDTQKELYGLKNELNQLENTLNNRTFDYQKNNETIENLTNQIAEFSDLEDTKKLYKELED 482
Cdd:PRK12704 100 ----RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEKVEE 165
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
202-1056 |
1.24e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 202 KAKKELSQAREYIEKIDIRINEVRANLEKlKKEKEDAEKYTVYNKKLKVTKYILTSKKVEFLKMVLDETKDEIEALKETK 281
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITS-KEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 282 NCYIQDISNIDSEIIGLKVKINELVNELNEKGSEEVMELHKSI----KELEVN------LNNDKNALENAID--DLKHTL 349
Cdd:TIGR00606 279 KQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELvdcqRELEKLnkerrlLNQEKTELLVEQGrlQLQADR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 350 KMEESKNNDLnETKEKINNIRIDTLKKEAEAKVLIKEIEKLNEERQ------------NLEKKVEQSESQVKALKNQESK 417
Cdd:TIGR00606 359 HQEHIRARDS-LIQSLATRLELDGFERGPFSERQIKNFHTLVIERQedeaktaaqlcaDLQSKERLKQEQADEIRDEKKG 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 418 LSERINDTQKELYGLKNELNQLENTLNNRTFDYQKNNETIENLTNQIAEFSDLEDT------KKLYKELEDIAVELEFSK 491
Cdd:TIGR00606 438 LGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNsltetlKKEVKSLQNEKADLDRKL 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 492 KKLQEKITERNDSQSKLDNLHSEYVKENARIKTLKDMENFSLDRAVKGVLD-AKLPGVVDIAGNLAKTKGEY-----KTA 565
Cdd:TIGR00606 518 RKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYfPNKKQLEDWLHSKSKEINQTrdrlaKLN 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 566 IEVAGGARLNHIVVKKMDDGSRAINYLKQKRL----GRATFLPMDRIKGMDAKDISDTGIIGKAIDLveFDIKYTNVFKF 641
Cdd:TIGR00606 598 KELASLEQNKNHINNELESKEEQLSSYEDKLFdvcgSQDEESDLERLKEEIEKSSKQRAMLAGATAV--YSQFITQLTDE 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 642 IFGNTHIVDNLENAKK----LSLKYKARFVTLEGEVIEPSGAMVGGNIRRNSAI-KVDIDMKKLTNLSEDIKELEQILSN 716
Cdd:TIGR00606 676 NQSCCPVCQRVFQTEAelqeFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLgLAPGRQSIIDLKEKEIPELRNKLQK 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 717 VKDEIERLNNKINTCSTRKLELDNRLKIARD--------QEFKKEeiTKSNNLKIKELNMLNSKIDDEISeltdeKEILS 788
Cdd:TIGR00606 756 VNRDIQRLKNDIEEQETLLGTIMPEEESAKVcltdvtimERFQME--LKDVERKIAQQAAKLQGSDLDRT-----VQQVN 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 789 QKVQNLDNKLSEVMGQRERIVNEIKsyensELSKRIKEIDHKIRENESSKNTL-ENEIKKGAIlvKEVLIPKISELNSNI 867
Cdd:TIGR00606 829 QEKQEKQHELDTVVSKIELNRKLIQ-----DQQEQIQHLKSKTNELKSEKLQIgTNLQRRQQF--EEQLVELSTEVQSLI 901
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 868 KSLADKKNMFKNSVEIYKSNIESNSSILSDK---RGKYEELTKGLKDLTDKKECYELEIEN-LQNNKEE-LREKATDIdN 942
Cdd:TIGR00606 902 REIKDAKEQDSPLETFLEKDQQEKEELISSKetsNKKAQDKVNDIKEKVKNIHGYMKDIENkIQDGKDDyLKQKETEL-N 980
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 943 QVNVINVDRAKYETRLEEEERKLYLCDTLENIED--ISDEMIEETYSLEIDDLERNQALLESSIKKLEPVNMRAI----- 1015
Cdd:TIGR00606 981 TVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQErwLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEhqkle 1060
|
890 900 910 920
....*....|....*....|....*....|....*....|.
gi 33578097 1016 EDYDFINERYEELFGKRKEYEQEEGKYLQLISEVQKRKKET 1056
Cdd:TIGR00606 1061 ENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEE 1101
|
|
| recF |
PRK14079 |
recombination protein F; Provisional |
10-106 |
1.28e-03 |
|
recombination protein F; Provisional
Pssm-ID: 184491 [Multi-domain] Cd Length: 349 Bit Score: 42.46 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 10 KNFKSFKNTKLKIPDGFTAILGPNGSGKSNTIDGICFVLGktsaKSLRAGKFNQLITYHNGKRADYAEVTLFFDNINREI 89
Cdd:PRK14079 9 LNYRNLAPPTLAFPPGVTAVVGENAAGKTNLLEAIYLALT----GELPNGRLADLVRFGEGEAWVHAEVETGGGLSRLEV 84
|
90
....*....|....*..
gi 33578097 90 PIDSDKvgicRKVKLNG 106
Cdd:PRK14079 85 GLGPGR----RELKLDG 97
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
130-470 |
1.50e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 130 QKKTSKASKVEKRRRMKKNEVLDLLSKISliadgpniILQGDLLRIIDTSPNERRKILDEVSGVAEFDEKSEKAKKELSQ 209
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQIN--------DLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 210 AREYIEKIDIRINEVRANLEKLKKEKEDAEKYT-VYNKKLKVTKYILTSKKVEflkmvLDETKDEIEALKETKNCYIQDI 288
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTRESLETQLkVLSRSINKIKQNLEQKQKE-----LKSKEKELKKLNEEKKELEEKV 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 289 SNIDSEIIGLKVKINELVNELNEKGSEevmelhksIKELEVNLNNDKNALENaiDDLKhtlKMEESKNNDLNETKEKINN 368
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKEKESK--------ISDLEDELNKDDFELKK--ENLE---KEIDEKNKEIEELKQTQKS 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 369 IRIDTLKKEAEAKVLIKEIEKLNEERQNLEKKVEQSESQVKALKNQESKLSERINDTQKELYGLKNELNQLENTLNNRTF 448
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
330 340
....*....|....*....|..
gi 33578097 449 DYQKNNETIENLTNQIAEFSDL 470
Cdd:TIGR04523 660 KWPEIIKKIKESKTKIDDIIEL 681
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
4-84 |
1.55e-03 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 41.04 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSFKNTKLKIPDGFTAILGPNGSGKSNTIDGICFVLGKTSAKSLRAGKFNQLITyhNGKraDYAEVTLFFD 83
Cdd:cd03276 1 IESITLKNFMCHRHLQIEFGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLIK--DGE--SSAKITVTLK 76
|
.
gi 33578097 84 N 84
Cdd:cd03276 77 N 77
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
343-492 |
1.84e-03 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 41.45 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 343 DDLKHTLKMEESKNNDLNETKEKINNIRIDTLKKEAEAKVLIKEIEKLNEERQNLEKKVEQSESQVKALKNQESKLSEri 422
Cdd:pfam11932 13 ATLDQALDLAEKAVAAAAQSQKKIDKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQIEEIER-- 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33578097 423 ndTQKELYGL-KNELNQLENTLNNRT-FDYQKNNETIENLTNQIAEfSDLEDTKKLYKELEDIAVELEFSKK 492
Cdd:pfam11932 91 --TERELVPLmLKMLDRLEQFVALDLpFLLEERQARLARLRELMDD-ADVSLAEKYRRILEAYQVEAEYGRT 159
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
267-466 |
1.98e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 267 LDETKDEIEALKETKNCYIQDISNIDSEIIGLKVKINELVNELNEKgSEEVMELHKSIKELEVNLNNDKNALENAIDDLK 346
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-QAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 347 HTLKME-------ESKN-NDLNEtkekinniRIDTLKKEAEAKVliKEIEKLNEERQNLEKKVEQSESQVKALKNQESKL 418
Cdd:COG3883 97 RSGGSVsyldvllGSESfSDFLD--------RLSALSKIADADA--DLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 33578097 419 SErindtqkelygLKNELN----QLENTLNNRTFDYQKNNETIENLTNQIAE 466
Cdd:COG3883 167 EA-----------AKAELEaqqaEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1112-1195 |
2.52e-03 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 42.13 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1112 SGGEKSLTALAflfaiqR--LNPSPFYVLDEVDAALDTKNASLIGDMISNASKESQFIVISHREQMISKSNVMYgvCMEN 1189
Cdd:COG2274 613 SGGQRQRLAIA------RalLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRII--VLDK 684
|
....*.
gi 33578097 1190 GlsKIV 1195
Cdd:COG2274 685 G--RIV 688
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
4-430 |
2.74e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.98 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 4 ISEIHLKNFKSFKNTKLKIPDGFTAILGPNGSGKSNTIDGICFVLG-KTSAKSLRAGkfnqlityhngkrADYAEVTLFF 82
Cdd:COG0497 2 LTELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALGLLLGgRADASLVRHG-------------ADKAEVEAVF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 83 DN----------INREIPIDSDKVGICRKVKLNGDNNYYVvwyevekQNTKINtessqkktskaskvekrrrmkknevLD 152
Cdd:COG0497 69 DLsddpplaawlEENGLDLDDGELILRREISADGRSRAFI-------NGRPVT-------------------------LS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 153 LLSKIS--LIadgpNIILQGDLLRIIDtsPNERRKILDEVSGvaefdekSEKAKKELSQAREyiekidiRINEVRANLEK 230
Cdd:COG0497 117 QLRELGelLV----DIHGQHEHQSLLD--PDAQRELLDAFAG-------LEELLEEYREAYR-------AWRALKKELEE 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 231 LKKEKEDAEKytvynkklkvtkyiltskKVEFLKMVLDE------TKDEIEALKETkncyIQDISNIDSeiigLKVKINE 304
Cdd:COG0497 177 LRADEAERAR------------------ELDLLRFQLEEleaaalQPGEEEELEEE----RRRLSNAEK----LREALQE 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 305 LVNELNEKGS-------------EEVMELHKSIKELEVNLNNDKNALENAIDDLKHTLKMEESKNNDLNETKEKINNIR- 370
Cdd:COG0497 231 ALEALSGGEGgaldllgqalralERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALLRr 310
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33578097 371 --------IDTL---KKEAEAKvlIKEIEKLNEERQNLEKKVEQSESQVKAL--------KNQESKLSERINDTQKELY 430
Cdd:COG0497 311 larkygvtVEELlayAEELRAE--LAELENSDERLEELEAELAEAEAELLEAaeklsaarKKAAKKLEKAVTAELADLG 387
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
295-429 |
3.83e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 295 IIGLKVKINELVNELNE------KGSEEVMELHKSIKELEVNLNNDKNALENAIDDlkhtlkMEESKNNDLNETKEKInn 368
Cdd:smart00787 142 LEGLKEGLDENLEGLKEdykllmKELELLNSIKPKLRDRKDALEEELRQLKQLEDE------LEDCDPTELDRAKEKL-- 213
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33578097 369 iridtlkkeaeaKVLIKEIEKLNEERQNLEKKVEQSESQVKALKNQESKLSERINDTQKEL 429
Cdd:smart00787 214 ------------KKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKL 262
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
317-563 |
4.03e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 317 VMELHKSIKELEVNLNNdknaLENAIDDLKHTLKMEESKNNDLNETKEKInnirIDTLKKEAEAkvLIKEIEKLNEERQN 396
Cdd:PHA02562 176 IRELNQQIQTLDMKIDH----IQQQIKTYNKNIEEQRKKNGENIARKQNK----YDELVEEAKT--IKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 397 LEKKVEQSESQVKALKNQESKLSERINDTQKELyglknELNQLENTLNNRTFDYQKNNETIENLTNQIAEFS-DLEDTKK 475
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVI-----KMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQhSLEKLDT 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 476 LYKELEDIAVELefskKKLQEKITERNDSQSKLDNLHSEYVKENARIKtlKDMENFSLDRAVKgvlDAKLPGVVDIAGNL 555
Cdd:PHA02562 321 AIDELEEIMDEF----NEQSKKLLELKNKISTNKQSLITLVDKAKKVK--AAIEELQAEFVDN---AEELAKLQDELDKI 391
|
....*...
gi 33578097 556 AKTKGEYK 563
Cdd:PHA02562 392 VKTKSELV 399
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
833-1056 |
4.21e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 833 ENESSKNTLENEIKkgAILVKEVLipkiselnsnikslADKKNMFKNSVEIYKSNIEsNSSILSDKRGKYEELTKGLKDL 912
Cdd:COG4717 31 PNEAGKSTLLAFIR--AMLLERLE--------------KEADELFKPQGRKPELNLK-ELKELEEELKEAEEKEEEYAEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 913 TDKKECYELEIENLQNNKEELREKATDIDNQVNVINV--DRAKYETRLEEEERKLylcDTLENIEDISDEMIEETYSLEi 990
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERL---EELEERLEELRELEEELEELE- 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33578097 991 DDLERNQALLESSIKKLEPVNMRAIEDydfINERYEELFGKRKEYEQEEGKYLQLISEVQKRKKET 1056
Cdd:COG4717 170 AELAELQEELEELLEQLSLATEEELQD---LAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
405-527 |
4.24e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 405 ESQVKALKNQESKLSERINDTQKELYGLKNELNQLENTLNNRTFDYQKNNETIENLTNQIAEFSDLEDTKKLYKELEDIA 484
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQ 95
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 33578097 485 VELEFSKKKLQEKITERNDSQSKLDNLHSEYVKENARIKTLKD 527
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
362-465 |
4.46e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 362 TKEKINNiRIDTLKK----EAEAKVLIKEIEklneERQNLEKKVEQSESQVKALKNQESKLSERINDTQKELYGLKNELN 437
Cdd:PRK11281 37 TEADVQA-QLDALNKqkllEAEDKLVQQDLE----QTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDND 111
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 33578097 438 -------------QLENTLNNRTFDYQKNNETIENLTNQIA 465
Cdd:PRK11281 112 eetretlstlslrQLESRLAQTLDQLQNAQNDLAEYNSQLV 152
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
736-948 |
4.49e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 41.18 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 736 LELDNR-LKIARDQEFKK-----EEITKsnnlKIKELNMLNSKIDDEISELTDEKEILSQKVQNLDNKLSEVmgqreriv 809
Cdd:pfam10168 534 LQLLSRaTQVFREEYLKKhdlarEEIQK----RVKLLKLQKEQQLQELQSLEEERKSLSERAEKLAEKYEEI-------- 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 810 neikSYENSELSKRIKEIDHKIRENESSKNTLENEIKKGAILVKEvlipKISELNSNIKSLADKKNMFKNSVEIYKSNIE 889
Cdd:pfam10168 602 ----KDKQEKLMRRCKKVLQRLNSQLPVLSDAEREMKKELETINE----QLKHLANAIKQAKKKMNYQRYQIAKSQSIRK 673
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 33578097 890 SNSSILSDKRGKyeeltkglkdltdkkecyeleienlqNNKEELREKATDIDNQVNVIN 948
Cdd:pfam10168 674 KSSLSLSEKQRK--------------------------TIKEILKQLGSEIDELIKQVK 706
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-38 |
4.49e-03 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 40.45 E-value: 4.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 33578097 1 MISISEIHlknfKSFKNTK------LKIPDG-FTAILGPNGSGKS 38
Cdd:COG4604 1 MIEIKNVS----KRYGGKVvlddvsLTIPKGgITALIGPNGAGKS 41
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
20-38 |
4.54e-03 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 40.41 E-value: 4.54e-03
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-38 |
5.14e-03 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 40.07 E-value: 5.14e-03
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
377-491 |
5.16e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.39 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 377 EAEAKVLIKEIEKLNEERQNLEKKVEQSESQVKALKNQES-----------KLSERINDTQKELYGLKNELNQLENTLNN 445
Cdd:smart00787 157 KEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDeledcdpteldRAKEKLKKLLQEIMIKVKKLEELEEELQE 236
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 33578097 446 RTFDYQKNNETIENLTNQIAEFSDLEDTKKLYKELEDIAVELEFSK 491
Cdd:smart00787 237 LESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKL 282
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
305-568 |
5.33e-03 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 40.91 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 305 LVNELNEKGSEeVMELHKSIKELevnLNNDKNALENAIDDLKHTLKMEESKNNDlnETKEKINNIRIDTLKKEAEAKVLI 384
Cdd:pfam18971 561 LENKLTAKGLS-LQEANKLIKDF---LSSNKELAGKALNFNKAVAEAKSTGNYD--EVKKAQKDLEKSLRKREHLEKEVE 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 385 KEIEKLNEERQNLEKKVEQS--ESQVKALKNQESKLSERINDTQKELYGLKNELNQLENTLNNRTFDYQKNNETIENLTN 462
Cdd:pfam18971 635 KKLESKSGNKNKMEAKAQANsqKDEIFALINKEANRDARAIAYTQNLKGIKRELSDKLEKISKDLKDFSKSFDEFKNGKN 714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 463 QiaEFSDLEDT-KKLYKELEDIAVELEFskkklqekITERNDSQSKLDNLHSEYVKENARIKTLK-DMENFSLDRAVKGV 540
Cdd:pfam18971 715 K--DFSKAEETlKALKGSVKDLGINPEW--------ISKVENLNAALNEFKNGKNKDFSKVTQAKsDLENSVKDVIINQK 784
|
250 260
....*....|....*....|....*...
gi 33578097 541 LDAKLPGvVDIAGNLAKTKGEYKTAIEV 568
Cdd:pfam18971 785 VTDKVDN-LNQAVSVAKAMGDFSRVEQV 811
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1105-1195 |
5.41e-03 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 39.43 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 1105 LQNLDV-MSGGEKSLTALAFLFAiqrLNPSpFYVLDEVDAALDTKNASLIGDMISN-ASKESQFIVISHREQMISKSNVM 1182
Cdd:cd03217 98 LRYVNEgFSGGEKKRNEILQLLL---LEPD-LAILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHYQRLLDYIKPD 173
|
90
....*....|...
gi 33578097 1183 YGVCMENGlsKIV 1195
Cdd:cd03217 174 RVHVLYDG--RIV 184
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-44 |
5.73e-03 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 40.44 E-value: 5.73e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 33578097 5 SEIHLKNF-KSFKNTK------LKIPDG-FTAILGPNGSGKS---NTIDGI 44
Cdd:COG3839 2 ASLELENVsKSYGGVEalkdidLDIEDGeFLVLLGPSGCGKStllRMIAGL 52
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
389-530 |
5.95e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 389 KLNEERQNLEKKVEQSESQVKALK-----NQESKLSERINDTQKELYGLKNELNQLENTLNNRTFDYQKNNETIENLTNQ 463
Cdd:PRK12704 32 KIKEAEEEAKRILEEAKKEAEAIKkeallEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEE 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33578097 464 iaefsdLEDTKKLYKELEDiavELEFSKKKLQEKITERNDsqsKLDNLhSEYVKENARIKTLKDMEN 530
Cdd:PRK12704 112 ------LEKKEKELEQKQQ---ELEKKEEELEELIEEQLQ---ELERI-SGLTAEEAKEILLEKVEE 165
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
181-530 |
6.38e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.71 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 181 NERRKILDEVSGVAEFDEKSEKAKKELSQAREYIEKIDIRINEVRANLEKLKKEKEDAEKYTVYNKKLKVTKYILTSKKV 260
Cdd:COG5185 173 NQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTS 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 261 EFLKMVLDETKDEIEALKETKNCYIQDISNIDSEIIG----LKVKINELVNELNEKGSEEVMELHKSIKELEVNLNNDKN 336
Cdd:COG5185 253 DKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKqfenTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKR 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 337 ALENAIDDLKHTLkmeESKNNDLNETKEKINNiRIDTLKKEAEakvLIKEIEKLNEERQNLEKKVEQSESQVKALKNQES 416
Cdd:COG5185 333 ETETGIQNLTAEI---EQGQESLTENLEAIKE-EIENIVGEVE---LSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQ 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 417 KLSERINDTQKELYGLKNELNQLENTLNNRTFDYQKNNETIENLTNQIAEFSDLEDTKKLYKELEDIAVELEFSKKKLQE 496
Cdd:COG5185 406 EILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNE 485
|
330 340 350
....*....|....*....|....*....|....*
gi 33578097 497 KITERNDSQSKL-DNLHSEYVKENARIKTLKDMEN 530
Cdd:COG5185 486 ELTQIESRVSTLkATLEKLRAKLERQLEGVRSKLD 520
|
|
| COG5391 |
COG5391 |
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ... |
256-467 |
6.46e-03 |
|
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];
Pssm-ID: 227680 [Multi-domain] Cd Length: 524 Bit Score: 40.55 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 256 TSKKVEFLKMVLDETKDEIEALKETKNCYIQ-DISNIDSEII---GLKVKINELVNElnekGSEEVMELHKSIKELEVNL 331
Cdd:COG5391 299 ILSIFSLFEKILIQLESEEESLTRLLESLNNlLLLVLNFSGVfakRLEQNQNSILNE----GVVQAETLRSSLKELLTQL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 332 NNDKNALENAIDDLKHTLKMEESKNNDLNETKEKINNiridtlkkeaeakvliKEIEKLNEERQNLEKKVEQSESQVKAL 411
Cdd:COG5391 375 QDEIKSRESLILTDSNLEKLTDQNLEDVEELSRSLRK----------------NSSQRAVVSQQPEGLTSFSKLSYKLRD 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33578097 412 KNQESKLSERINDTQKELYGLKNELNQLE------NTLNNRTFDYQKN------NETIENLTNQIAEF 467
Cdd:COG5391 439 FVQEKSRSKSIESLQQDKEKLEEQLAIAEkdaqeiNEELKNELKFFFSvrnsdlEKILKSVADSHIEW 506
|
|
| auto_Ata |
NF033481 |
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ... |
286-583 |
8.75e-03 |
|
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 40.62 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 286 QDISNIDSEIIGLKVKINELVNELNEKGSEEVMELHKSIKELEVNLNNDKNALENAIDDLKHTLkmeeskNNDLNETKEK 365
Cdd:NF033481 786 QNITNLNQKLDDTKTNLGNQITDTNKNLNDAKKDLGNQITDTNTKLNTTKDQLTTQINDTKTEL------NNTIGNTKTE 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 366 INNiRIDTLKKEAE-----------AKVLIKEIEKLN-------------EERQNLEKKVEQSESQVKALKNQE------ 415
Cdd:NF033481 860 LNT-KIDNTKTELEnkglnfagnsgADVHRKLGDKLNivggaaastpaakTSGENVITRTTQDGIQIELLKDSKfdsvtt 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 416 ----------------SKLSERINDTQKELYGLK-----------NELNQLENTLNNRTFDYQKN-NETIENLTNQIAEF 467
Cdd:NF033481 939 gnttlntngltikegpSITKQGINAGSKQITNVAdginakdavnvDQLTKVKENLNGRITDTNNQlNDAKKDLGNQIADT 1018
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 468 S-DLEDTKK-LYKELEDIAVELEFSKKKLQEKIterNDSQSKLDNLHSEyVKENARIKTLKDMENFSLDRAVKGVLDAKL 545
Cdd:NF033481 1019 NkNLNDAKKdLGDQITDTNTKLNNTKDQLTTQI---NDTKTELNNTIGN-TKTELENKGLNFAGNSGADVHRKLGDKLNI 1094
|
330 340 350
....*....|....*....|....*....|....*...
gi 33578097 546 PGVVDIAGNLAKTKGEYKTAIEVAGGARLNHIVVKKMD 583
Cdd:NF033481 1095 VGGAAASTPAAKTSGENVITRTTKDGIQIELLKDSKFD 1132
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
292-444 |
8.91e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.26 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 292 DSEIIGLKVKINELVNELNE--KGSEEVMELHKSIKELEVNLNNDKNALenaiddlkhtLKMEESKNNDLNETKEKINNI 369
Cdd:pfam07888 72 ERQRRELESRVAELKEELRQsrEKHEELEEKYKELSASSEELSEEKDAL----------LAQRAAHEARIRELEEDIKTL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 370 RIDTLKKEAEAKVLIKEIEKL-------NEERQNLEKKVEQSESQVKALKNQESKLSERINDTQKELYGLKNELNQLENT 442
Cdd:pfam07888 142 TQRVLERETELERMKERAKKAgaqrkeeEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQK 221
|
..
gi 33578097 443 LN 444
Cdd:pfam07888 222 LT 223
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
201-508 |
8.97e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.48 E-value: 8.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 201 EKAKKELSQAREYIEKIDIRINEVRANLEKLK----------KEKEDAEKYTVYNKKLKVTKYILTSKKVEFLKMVLDET 270
Cdd:pfam05483 229 EEYKKEINDKEKQVSLLLIQITEKENKMKDLTflleesrdkaNQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRS 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 271 KDEIEALKETKNCYIQDISNIDSEiiglKVKINELVNELNEKGSEEVMELHKSIKELEVNLNNDKNALENAIDDLKHTLK 350
Cdd:pfam05483 309 MSTQKALEEDLQIATKTICQLTEE----KEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITM 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 351 MEESKNNDLNETKEKINNIRIDTlkkeAEAKVLIKEIEKLNEERQNLEKKVEQsesqvkaLKNQESKLSERINDTQKELY 430
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVEL----EELKKILAEDEKLLDEKKQFEKIAEE-------LKGKEQELIFLLQAREKEIH 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 431 GLKNELNQLENTLNNRTFDYQKNNETIENLTNQIAEFSD-----LEDTKKLYKELEDIAVELefskKKLQEKITERNDSQ 505
Cdd:pfam05483 454 DLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAhcdklLLENKELTQEASDMTLEL----KKHQEDIINCKKQE 529
|
...
gi 33578097 506 SKL 508
Cdd:pfam05483 530 ERM 532
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
16-38 |
9.26e-03 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 39.05 E-value: 9.26e-03
10 20
....*....|....*....|....
gi 33578097 16 KNTKLKIPDG-FTAILGPNGSGKS 38
Cdd:cd03235 16 EDVSFEVKPGeFLAIVGPNGAGKS 39
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
695-966 |
9.62e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 40.04 E-value: 9.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 695 IDMKKLTNLSEDIKELEQILSN---VKDEIERLNNKINTC----STRKLELDNRLKIARDQEFK------KEEITKSNNL 761
Cdd:pfam13166 219 ILIQKVIGKSSAIEELIKNPDLadwVEQGLELHKAHLDTCpfcgQPLPAERKAALEAHFDDEFTefqnrlQKLIEKVESA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 762 KIKELNMLNSKIDDEI--SELTDEKEILSQKVQNLDNKLSEVMGqrerivneiksyensELSKRIKEIDHKIrENESSKN 839
Cdd:pfam13166 299 ISSLLAQLPAVSDLASllSAFELDVEDIESEAEVLNSQLDGLRR---------------ALEAKRKDPFKSI-ELDSVDA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33578097 840 TLENEIKKGAILVKEvlipkISELNSNIKSLADKKNMFKNSVEiyKSNIESNSSILSDKRGKYEELTKGLKDLTDKKECY 919
Cdd:pfam13166 363 KIESINDLVASINEL-----IAKHNEITDNFEEEKNKAKKKLR--LHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNL 435
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 33578097 920 ELEIENLQNNKEELREKATDIDNQVNVINVDRAKYE-TRLE---EEERKLY 966
Cdd:pfam13166 436 EAEIKKLREEIKELEAQLRDHKPGADEINKLLKAFGfGELElsfNEEGKGY 486
|
|
| |
